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    Jena Bioscience cytidine
    Cytidine, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 94/100, based on 65 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ( A ) Domain organisation of La and LARP7 proteins ( , , ), Tetrahymena Mlp1 is based on Alphafold3 domain predictions and sequence alignments (Figure S5A) and includes an apparent additional xRRM in a region known to bind RNA . Domains are as annotated, ‘+’ or ‘-‘ indicates regions of the sequence with correspondingly charged residues at neutral pH. ( B ) AtLa1 EMSA using 1% agarose gel with 80 nM AtTR 1-268 and protein concentrations (nM) as annotated, visualized by fluorescent staining. ( C ) Representative AtLa1 EMSAs with pre-tsnoR43.1, pretsnoR43.1ΔU and snoR43.1 substrates ( , ), as annotated, conditions as (B). White lines have been added to separate panels from the same gel. ( D ) ELISA experiments detecting immunolabelled AtLa1 bound to ≤0.5 pmol biotinylated AtTR 1-268 and non-biotinylated competitor RNA as annotated, (ytRNA, budding yeast tRNA). Lines show equations fit to data used to calculate K D , average AtTR values are shown in all experiments for comparison, error bars are the standard deviation. ( E ) ELISA experiments as (D) with plant TR competitors (full details in Table S2). ( F ) Comparison of AtLa1-AtTR binding assays used in this work. Solid black circles are average initial capillary fluorescence values (upper panel) or 1.5 s T-jump data (lower panel) from MST experiments, signal is from 5 nM <t>3’</t> <t>Cy5-labelled</t> AtTR 1-268. Solid lines show equations fit to data used to calculate K D (Table S3), dotted lines for both fast processes are Hill equation fits with n=2 for comparison, error bars are standard deviation. Open black circles with dashed lines are normalised fluorescence emission at 680 nM from 20 nM AtTR-Cy5, with excitation at 625 nM using a traditional spectrofluorometer (full spectra in Fig. S1H). Closed red circles show normalised Δε at 265 nM from circular dichroism experiments monitoring 50 nM unlabelled AtTR (difference spectra in Fig. S1I). Blue closed circles are normalised fractional saturation of 40 nM unlabelled AtTR calculated from band shift distances for EMSAs (Fig. S1J) and open blue circles and dotted lines are 1/normalised signal change for ELISA competition experiments (derived from (D) for comparison). For all experiments other than ELISAs, AtLa1 concentrations are divided by the fold increase in AtTR concentration. ( G ) MST experiments detecting AtTR-Cy5 in the presence of excess unlabelled competitor RNA as annotated (Table S4), AtTR-AtLa1 data are reproduced from (F) for comparison.
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    ( A ) Domain organisation of La and LARP7 proteins ( , , ), Tetrahymena Mlp1 is based on Alphafold3 domain predictions and sequence alignments (Figure S5A) and includes an apparent additional xRRM in a region known to bind RNA . Domains are as annotated, ‘+’ or ‘-‘ indicates regions of the sequence with correspondingly charged residues at neutral pH. ( B ) AtLa1 EMSA using 1% agarose gel with 80 nM AtTR 1-268 and protein concentrations (nM) as annotated, visualized by fluorescent staining. ( C ) Representative AtLa1 EMSAs with pre-tsnoR43.1, pretsnoR43.1ΔU and snoR43.1 substrates ( , ), as annotated, conditions as (B). White lines have been added to separate panels from the same gel. ( D ) ELISA experiments detecting immunolabelled AtLa1 bound to ≤0.5 pmol biotinylated AtTR 1-268 and non-biotinylated competitor RNA as annotated, (ytRNA, budding yeast tRNA). Lines show equations fit to data used to calculate K D , average AtTR values are shown in all experiments for comparison, error bars are the standard deviation. ( E ) ELISA experiments as (D) with plant TR competitors (full details in Table S2). ( F ) Comparison of AtLa1-AtTR binding assays used in this work. Solid black circles are average initial capillary fluorescence values (upper panel) or 1.5 s T-jump data (lower panel) from MST experiments, signal is from 5 nM 3’ <t>Cy5-labelled</t> AtTR 1-268. Solid lines show equations fit to data used to calculate K D (Table S3), dotted lines for both fast processes are Hill equation fits with n=2 for comparison, error bars are standard deviation. Open black circles with dashed lines are normalised fluorescence emission at 680 nM from 20 nM <t>AtTR-Cy5,</t> with excitation at 625 nM using a traditional spectrofluorometer (full spectra in Fig. S1H). Closed red circles show normalised Δε at 265 nM from circular dichroism experiments monitoring 50 nM unlabelled AtTR (difference spectra in Fig. S1I). Blue closed circles are normalised fractional saturation of 40 nM unlabelled AtTR calculated from band shift distances for EMSAs (Fig. S1J) and open blue circles and dotted lines are 1/normalised signal change for ELISA competition experiments (derived from (D) for comparison). For all experiments other than ELISAs, AtLa1 concentrations are divided by the fold increase in AtTR concentration. ( G ) MST experiments detecting AtTR-Cy5 in the presence of excess unlabelled competitor RNA as annotated (Table S4), AtTR-AtLa1 data are reproduced from (F) for comparison.
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    ( A ) Domain organisation of La and LARP7 proteins ( , , ), Tetrahymena Mlp1 is based on Alphafold3 domain predictions and sequence alignments (Figure S5A) and includes an apparent additional xRRM in a region known to bind RNA . Domains are as annotated, ‘+’ or ‘-‘ indicates regions of the sequence with correspondingly charged residues at neutral pH. ( B ) AtLa1 EMSA using 1% agarose gel with 80 nM AtTR 1-268 and protein concentrations (nM) as annotated, visualized by fluorescent staining. ( C ) Representative AtLa1 EMSAs with pre-tsnoR43.1, pretsnoR43.1ΔU and snoR43.1 substrates ( , ), as annotated, conditions as (B). White lines have been added to separate panels from the same gel. ( D ) ELISA experiments detecting immunolabelled AtLa1 bound to ≤0.5 pmol biotinylated AtTR 1-268 and non-biotinylated competitor RNA as annotated, (ytRNA, budding yeast tRNA). Lines show equations fit to data used to calculate K D , average AtTR values are shown in all experiments for comparison, error bars are the standard deviation. ( E ) ELISA experiments as (D) with plant TR competitors (full details in Table S2). ( F ) Comparison of AtLa1-AtTR binding assays used in this work. Solid black circles are average initial capillary fluorescence values (upper panel) or 1.5 s T-jump data (lower panel) from MST experiments, signal is from 5 nM 3’ <t>Cy5-labelled</t> AtTR 1-268. Solid lines show equations fit to data used to calculate K D (Table S3), dotted lines for both fast processes are Hill equation fits with n=2 for comparison, error bars are standard deviation. Open black circles with dashed lines are normalised fluorescence emission at 680 nM from 20 nM <t>AtTR-Cy5,</t> with excitation at 625 nM using a traditional spectrofluorometer (full spectra in Fig. S1H). Closed red circles show normalised Δε at 265 nM from circular dichroism experiments monitoring 50 nM unlabelled AtTR (difference spectra in Fig. S1I). Blue closed circles are normalised fractional saturation of 40 nM unlabelled AtTR calculated from band shift distances for EMSAs (Fig. S1J) and open blue circles and dotted lines are 1/normalised signal change for ELISA competition experiments (derived from (D) for comparison). For all experiments other than ELISAs, AtLa1 concentrations are divided by the fold increase in AtTR concentration. ( G ) MST experiments detecting AtTR-Cy5 in the presence of excess unlabelled competitor RNA as annotated (Table S4), AtTR-AtLa1 data are reproduced from (F) for comparison.
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    ( A ) Domain organisation of La and LARP7 proteins ( , , ), Tetrahymena Mlp1 is based on Alphafold3 domain predictions and sequence alignments (Figure S5A) and includes an apparent additional xRRM in a region known to bind RNA . Domains are as annotated, ‘+’ or ‘-‘ indicates regions of the sequence with correspondingly charged residues at neutral pH. ( B ) AtLa1 EMSA using 1% agarose gel with 80 nM AtTR 1-268 and protein concentrations (nM) as annotated, visualized by fluorescent staining. ( C ) Representative AtLa1 EMSAs with pre-tsnoR43.1, pretsnoR43.1ΔU and snoR43.1 substrates ( , ), as annotated, conditions as (B). White lines have been added to separate panels from the same gel. ( D ) ELISA experiments detecting immunolabelled AtLa1 bound to ≤0.5 pmol biotinylated AtTR 1-268 and non-biotinylated competitor RNA as annotated, (ytRNA, budding yeast tRNA). Lines show equations fit to data used to calculate K D , average AtTR values are shown in all experiments for comparison, error bars are the standard deviation. ( E ) ELISA experiments as (D) with plant TR competitors (full details in Table S2). ( F ) Comparison of AtLa1-AtTR binding assays used in this work. Solid black circles are average initial capillary fluorescence values (upper panel) or 1.5 s T-jump data (lower panel) from MST experiments, signal is from 5 nM 3’ Cy5-labelled AtTR 1-268. Solid lines show equations fit to data used to calculate K D (Table S3), dotted lines for both fast processes are Hill equation fits with n=2 for comparison, error bars are standard deviation. Open black circles with dashed lines are normalised fluorescence emission at 680 nM from 20 nM AtTR-Cy5, with excitation at 625 nM using a traditional spectrofluorometer (full spectra in Fig. S1H). Closed red circles show normalised Δε at 265 nM from circular dichroism experiments monitoring 50 nM unlabelled AtTR (difference spectra in Fig. S1I). Blue closed circles are normalised fractional saturation of 40 nM unlabelled AtTR calculated from band shift distances for EMSAs (Fig. S1J) and open blue circles and dotted lines are 1/normalised signal change for ELISA competition experiments (derived from (D) for comparison). For all experiments other than ELISAs, AtLa1 concentrations are divided by the fold increase in AtTR concentration. ( G ) MST experiments detecting AtTR-Cy5 in the presence of excess unlabelled competitor RNA as annotated (Table S4), AtTR-AtLa1 data are reproduced from (F) for comparison.

    Journal: bioRxiv

    Article Title: La protein binding to telomerase RNA supports an evolutionary relationship between plant and ciliate telomerase pathways

    doi: 10.64898/2026.01.19.700320

    Figure Lengend Snippet: ( A ) Domain organisation of La and LARP7 proteins ( , , ), Tetrahymena Mlp1 is based on Alphafold3 domain predictions and sequence alignments (Figure S5A) and includes an apparent additional xRRM in a region known to bind RNA . Domains are as annotated, ‘+’ or ‘-‘ indicates regions of the sequence with correspondingly charged residues at neutral pH. ( B ) AtLa1 EMSA using 1% agarose gel with 80 nM AtTR 1-268 and protein concentrations (nM) as annotated, visualized by fluorescent staining. ( C ) Representative AtLa1 EMSAs with pre-tsnoR43.1, pretsnoR43.1ΔU and snoR43.1 substrates ( , ), as annotated, conditions as (B). White lines have been added to separate panels from the same gel. ( D ) ELISA experiments detecting immunolabelled AtLa1 bound to ≤0.5 pmol biotinylated AtTR 1-268 and non-biotinylated competitor RNA as annotated, (ytRNA, budding yeast tRNA). Lines show equations fit to data used to calculate K D , average AtTR values are shown in all experiments for comparison, error bars are the standard deviation. ( E ) ELISA experiments as (D) with plant TR competitors (full details in Table S2). ( F ) Comparison of AtLa1-AtTR binding assays used in this work. Solid black circles are average initial capillary fluorescence values (upper panel) or 1.5 s T-jump data (lower panel) from MST experiments, signal is from 5 nM 3’ Cy5-labelled AtTR 1-268. Solid lines show equations fit to data used to calculate K D (Table S3), dotted lines for both fast processes are Hill equation fits with n=2 for comparison, error bars are standard deviation. Open black circles with dashed lines are normalised fluorescence emission at 680 nM from 20 nM AtTR-Cy5, with excitation at 625 nM using a traditional spectrofluorometer (full spectra in Fig. S1H). Closed red circles show normalised Δε at 265 nM from circular dichroism experiments monitoring 50 nM unlabelled AtTR (difference spectra in Fig. S1I). Blue closed circles are normalised fractional saturation of 40 nM unlabelled AtTR calculated from band shift distances for EMSAs (Fig. S1J) and open blue circles and dotted lines are 1/normalised signal change for ELISA competition experiments (derived from (D) for comparison). For all experiments other than ELISAs, AtLa1 concentrations are divided by the fold increase in AtTR concentration. ( G ) MST experiments detecting AtTR-Cy5 in the presence of excess unlabelled competitor RNA as annotated (Table S4), AtTR-AtLa1 data are reproduced from (F) for comparison.

    Article Snippet: For ELISA or MST experiments, synthesised RNA was 3’ labelled with biotin- or Cy5-labelled cytosine bisphosphate, respectively (Thermo Scientific #20160, Jena Biosciences #NU-1706-CY5), using PierceTM RNA 3’ End Biotinylation Kit (Thermo Scientific, #20160) according to the manufacturer’s instructions.

    Techniques: Sequencing, Agarose Gel Electrophoresis, Staining, Enzyme-linked Immunosorbent Assay, Comparison, Standard Deviation, Binding Assay, Fluorescence, Circular Dichroism, Electrophoretic Mobility Shift Assay, Derivative Assay, Concentration Assay

    ( A,D ) Initial capillary fluorescence values from MST experiments for 5 nM 3’ Cy5-labelled AtTR 1-268 and (A) AtTERT minimal binding domain (TRBD) or (D) AtDomino, with or without constant AtLa1 as annotated. AtDomino average data are reproduced from , TRBD average data are reproduced from Figure S4E. Lines show fittings used to calculate K D values, error bars represent standard deviation. ( B ) Multicomponent yeast three-hybrid experiments pairing AtTR 1-268 MS2 or MS2 only with AD constructs of AtTERT TRBD variants in the presence of AtLa1 BD or empty BD constructs, as annotated. Numbers refer to mM concentrations of 3-aminotriazole in growth media, letters refer to amino acids absent for growth. ( C,F ) Schemas of (C) partial AtTERT-TR-La1 complex omitting AtTERT TEN, RT and CTE domains, (F) possible AtTR-La1-Domino complex, with domains as annotated, LaM in grey, xRRM in red, DUF3223 in yellow, TRBD in pink and RNA-binding linker in cyan. ( E ) Mass photometry (MP) deconvoluted mass spectra of samples with AtLa1, AtLa1+AtDomino with or without AtTR, as annotated, Solid lines show Gaussian fittings with values in text, annotated with average mass values in kDa, numbers in grey are peaks which cannot be unambiguously assigned (more details in Table S5).

    Journal: bioRxiv

    Article Title: La protein binding to telomerase RNA supports an evolutionary relationship between plant and ciliate telomerase pathways

    doi: 10.64898/2026.01.19.700320

    Figure Lengend Snippet: ( A,D ) Initial capillary fluorescence values from MST experiments for 5 nM 3’ Cy5-labelled AtTR 1-268 and (A) AtTERT minimal binding domain (TRBD) or (D) AtDomino, with or without constant AtLa1 as annotated. AtDomino average data are reproduced from , TRBD average data are reproduced from Figure S4E. Lines show fittings used to calculate K D values, error bars represent standard deviation. ( B ) Multicomponent yeast three-hybrid experiments pairing AtTR 1-268 MS2 or MS2 only with AD constructs of AtTERT TRBD variants in the presence of AtLa1 BD or empty BD constructs, as annotated. Numbers refer to mM concentrations of 3-aminotriazole in growth media, letters refer to amino acids absent for growth. ( C,F ) Schemas of (C) partial AtTERT-TR-La1 complex omitting AtTERT TEN, RT and CTE domains, (F) possible AtTR-La1-Domino complex, with domains as annotated, LaM in grey, xRRM in red, DUF3223 in yellow, TRBD in pink and RNA-binding linker in cyan. ( E ) Mass photometry (MP) deconvoluted mass spectra of samples with AtLa1, AtLa1+AtDomino with or without AtTR, as annotated, Solid lines show Gaussian fittings with values in text, annotated with average mass values in kDa, numbers in grey are peaks which cannot be unambiguously assigned (more details in Table S5).

    Article Snippet: For ELISA or MST experiments, synthesised RNA was 3’ labelled with biotin- or Cy5-labelled cytosine bisphosphate, respectively (Thermo Scientific #20160, Jena Biosciences #NU-1706-CY5), using PierceTM RNA 3’ End Biotinylation Kit (Thermo Scientific, #20160) according to the manufacturer’s instructions.

    Techniques: Fluorescence, Binding Assay, Standard Deviation, Construct, RNA Binding Assay

    ( A ) Domain structure of AtLa1, including LaM (grey) and xRRM (red), as predicted by Alphafold2 , and visualized using ChimeraX . xRRM residues chosen for mutagenesis studies are shown in a magnified panel (the same colour scheme is used in B-E). ( B-E ) Binding of AtLa1 fragments (B, C) and AtLa1 xRRM point variants (D, E) to AtTR investigated by EMSA (B, D) and MST (C, E). (B, D) Representative band shift of 80 nM AtTR 1-268 caused by binding of AtLa1 protein constructs (concentrations in nM) is visualised in agarose gel by fluorescent staining. White lines have been added to separate panels in the same gel (full image in Figure S2). (C, E) Initial capillary fluorescence values from MST experiments (upper panels) or MST 1.5 s T-jump data (lower panels) for 3’ Cy5-labelled AtTR 1-268 and La1 fragments as indicated, with average AtLa1 FL data from reproduced for comparison. Open symbols and dashed lines in (C), lower panel only, show data in the presence of 100x excess unlabelled tRNA competitor. Lines show equations fit to data used to calculate K D , error bars are the standard deviation.

    Journal: bioRxiv

    Article Title: La protein binding to telomerase RNA supports an evolutionary relationship between plant and ciliate telomerase pathways

    doi: 10.64898/2026.01.19.700320

    Figure Lengend Snippet: ( A ) Domain structure of AtLa1, including LaM (grey) and xRRM (red), as predicted by Alphafold2 , and visualized using ChimeraX . xRRM residues chosen for mutagenesis studies are shown in a magnified panel (the same colour scheme is used in B-E). ( B-E ) Binding of AtLa1 fragments (B, C) and AtLa1 xRRM point variants (D, E) to AtTR investigated by EMSA (B, D) and MST (C, E). (B, D) Representative band shift of 80 nM AtTR 1-268 caused by binding of AtLa1 protein constructs (concentrations in nM) is visualised in agarose gel by fluorescent staining. White lines have been added to separate panels in the same gel (full image in Figure S2). (C, E) Initial capillary fluorescence values from MST experiments (upper panels) or MST 1.5 s T-jump data (lower panels) for 3’ Cy5-labelled AtTR 1-268 and La1 fragments as indicated, with average AtLa1 FL data from reproduced for comparison. Open symbols and dashed lines in (C), lower panel only, show data in the presence of 100x excess unlabelled tRNA competitor. Lines show equations fit to data used to calculate K D , error bars are the standard deviation.

    Article Snippet: For ELISA or MST experiments, synthesised RNA was 3’ labelled with biotin- or Cy5-labelled cytosine bisphosphate, respectively (Thermo Scientific #20160, Jena Biosciences #NU-1706-CY5), using PierceTM RNA 3’ End Biotinylation Kit (Thermo Scientific, #20160) according to the manufacturer’s instructions.

    Techniques: Mutagenesis, Binding Assay, Electrophoretic Mobility Shift Assay, Construct, Agarose Gel Electrophoresis, Staining, Fluorescence, Comparison, Standard Deviation

    ( A ) Overview and legend of representative AtTR constructs used in La1 binding experiments (B-E, additional constructs in Figure S6A), template (cyan) and deleted P4 (red) region are highlighted. ( B ) ELISA competition experiments detecting immunolabelled AtLa1 bound to ≤0.5 pmol biotinylated AtTR 1-268 and non-biotinylated competitor AtTR fragments. ( C, D, E ) Initial capillary fluorescence values from MST experiments (upper panel) or MST 1.5 s T-jump data (lower panel) for 5 nM 3’ Cy5-labelled AtTR fragments and La1 FL (C), LaM (D) or xRRM (E). Lines show equations fit to data used to calculate K D . ( F ) Schema of AtTR regions which bind AtLa1 LaM (grey) or xRRM (red) domains. Possible binding sites are shown in black, unlikely/nonspecific binding sites in light grey. ( G ) K D values from AtLa1 ELISA competition experiments as (B) but with varying AtTR 3’ termini. The line shows fitting to a Gaussian distribution centred on 275 nt, full details in Figure S3B-C.

    Journal: bioRxiv

    Article Title: La protein binding to telomerase RNA supports an evolutionary relationship between plant and ciliate telomerase pathways

    doi: 10.64898/2026.01.19.700320

    Figure Lengend Snippet: ( A ) Overview and legend of representative AtTR constructs used in La1 binding experiments (B-E, additional constructs in Figure S6A), template (cyan) and deleted P4 (red) region are highlighted. ( B ) ELISA competition experiments detecting immunolabelled AtLa1 bound to ≤0.5 pmol biotinylated AtTR 1-268 and non-biotinylated competitor AtTR fragments. ( C, D, E ) Initial capillary fluorescence values from MST experiments (upper panel) or MST 1.5 s T-jump data (lower panel) for 5 nM 3’ Cy5-labelled AtTR fragments and La1 FL (C), LaM (D) or xRRM (E). Lines show equations fit to data used to calculate K D . ( F ) Schema of AtTR regions which bind AtLa1 LaM (grey) or xRRM (red) domains. Possible binding sites are shown in black, unlikely/nonspecific binding sites in light grey. ( G ) K D values from AtLa1 ELISA competition experiments as (B) but with varying AtTR 3’ termini. The line shows fitting to a Gaussian distribution centred on 275 nt, full details in Figure S3B-C.

    Article Snippet: For ELISA or MST experiments, synthesised RNA was 3’ labelled with biotin- or Cy5-labelled cytosine bisphosphate, respectively (Thermo Scientific #20160, Jena Biosciences #NU-1706-CY5), using PierceTM RNA 3’ End Biotinylation Kit (Thermo Scientific, #20160) according to the manufacturer’s instructions.

    Techniques: Construct, Binding Assay, Enzyme-linked Immunosorbent Assay, Fluorescence

    ( A ) Alphafold3 prediction of AtLa1-AtDomino complex showing AtLa1 LaM (La motif and RRM, grey) and xRRM (red), and AtDomino DUF3223 (yellow) domains. Highlighted panel shows interacting AtLa1 residues (green) on the RRM-DUF3223 interface. Structural visualisations prepared using ChimeraX . ( B ) Yeast 2-hybrid and ( C ) semi-quantitative beta galactosidase assays pairing Gal4 binding domain (BD) fused AtLa1 fragments and variants with Gal4 activation domain (AD) fused AtDomino. For (B), numbers refer to mM concentrations of 3-aminotriazole in the growth media, letters refer to amino acids absent for growth. For (C), BD-fused AtLa1 (purple bars) are compared to empty BD (grey bars), error bars represent standard deviation. ( D ) In vitro ELISA detecting AtDomino bound to immobilised AtLa1 WT (black circles) and AtLa1 SYD124GGG (dark red stars). Lines show equations fit to data used to calculate K D . ( E ) Domain structure of AtLa1 and AtDomino showing protein-protein (black arrows) and protein-RNA interactions (green bars), predicted domains as annotated, ‘+’ or ‘-‘ indicates regions of the sequence with correspondingly charged residues at neutral pH. ( F ) Initial capillary fluorescence values (left) and MST 1.5 s T-jump data (right) for AtDomino (black diamonds) and AtDomino delC (green diamonds) with 5 nM 3’ Cy5-labelled AtTR 1-268. For comparison, AtDomino interaction with Cy5-AtTR in the presence of excess unlabelled ytRNA competitor (open black diamonds, dashed lines) is shown. Lines show equations fit to data used to calculate K D , error bars represent standard deviation.

    Journal: bioRxiv

    Article Title: La protein binding to telomerase RNA supports an evolutionary relationship between plant and ciliate telomerase pathways

    doi: 10.64898/2026.01.19.700320

    Figure Lengend Snippet: ( A ) Alphafold3 prediction of AtLa1-AtDomino complex showing AtLa1 LaM (La motif and RRM, grey) and xRRM (red), and AtDomino DUF3223 (yellow) domains. Highlighted panel shows interacting AtLa1 residues (green) on the RRM-DUF3223 interface. Structural visualisations prepared using ChimeraX . ( B ) Yeast 2-hybrid and ( C ) semi-quantitative beta galactosidase assays pairing Gal4 binding domain (BD) fused AtLa1 fragments and variants with Gal4 activation domain (AD) fused AtDomino. For (B), numbers refer to mM concentrations of 3-aminotriazole in the growth media, letters refer to amino acids absent for growth. For (C), BD-fused AtLa1 (purple bars) are compared to empty BD (grey bars), error bars represent standard deviation. ( D ) In vitro ELISA detecting AtDomino bound to immobilised AtLa1 WT (black circles) and AtLa1 SYD124GGG (dark red stars). Lines show equations fit to data used to calculate K D . ( E ) Domain structure of AtLa1 and AtDomino showing protein-protein (black arrows) and protein-RNA interactions (green bars), predicted domains as annotated, ‘+’ or ‘-‘ indicates regions of the sequence with correspondingly charged residues at neutral pH. ( F ) Initial capillary fluorescence values (left) and MST 1.5 s T-jump data (right) for AtDomino (black diamonds) and AtDomino delC (green diamonds) with 5 nM 3’ Cy5-labelled AtTR 1-268. For comparison, AtDomino interaction with Cy5-AtTR in the presence of excess unlabelled ytRNA competitor (open black diamonds, dashed lines) is shown. Lines show equations fit to data used to calculate K D , error bars represent standard deviation.

    Article Snippet: For ELISA or MST experiments, synthesised RNA was 3’ labelled with biotin- or Cy5-labelled cytosine bisphosphate, respectively (Thermo Scientific #20160, Jena Biosciences #NU-1706-CY5), using PierceTM RNA 3’ End Biotinylation Kit (Thermo Scientific, #20160) according to the manufacturer’s instructions.

    Techniques: Binding Assay, Activation Assay, Standard Deviation, In Vitro, Enzyme-linked Immunosorbent Assay, Sequencing, Fluorescence, Comparison

    ( A ) Domain organisation of La and LARP7 proteins ( , , ), Tetrahymena Mlp1 is based on Alphafold3 domain predictions and sequence alignments (Figure S5A) and includes an apparent additional xRRM in a region known to bind RNA . Domains are as annotated, ‘+’ or ‘-‘ indicates regions of the sequence with correspondingly charged residues at neutral pH. ( B ) AtLa1 EMSA using 1% agarose gel with 80 nM AtTR 1-268 and protein concentrations (nM) as annotated, visualized by fluorescent staining. ( C ) Representative AtLa1 EMSAs with pre-tsnoR43.1, pretsnoR43.1ΔU and snoR43.1 substrates ( , ), as annotated, conditions as (B). White lines have been added to separate panels from the same gel. ( D ) ELISA experiments detecting immunolabelled AtLa1 bound to ≤0.5 pmol biotinylated AtTR 1-268 and non-biotinylated competitor RNA as annotated, (ytRNA, budding yeast tRNA). Lines show equations fit to data used to calculate K D , average AtTR values are shown in all experiments for comparison, error bars are the standard deviation. ( E ) ELISA experiments as (D) with plant TR competitors (full details in Table S2). ( F ) Comparison of AtLa1-AtTR binding assays used in this work. Solid black circles are average initial capillary fluorescence values (upper panel) or 1.5 s T-jump data (lower panel) from MST experiments, signal is from 5 nM 3’ Cy5-labelled AtTR 1-268. Solid lines show equations fit to data used to calculate K D (Table S3), dotted lines for both fast processes are Hill equation fits with n=2 for comparison, error bars are standard deviation. Open black circles with dashed lines are normalised fluorescence emission at 680 nM from 20 nM AtTR-Cy5, with excitation at 625 nM using a traditional spectrofluorometer (full spectra in Fig. S1H). Closed red circles show normalised Δε at 265 nM from circular dichroism experiments monitoring 50 nM unlabelled AtTR (difference spectra in Fig. S1I). Blue closed circles are normalised fractional saturation of 40 nM unlabelled AtTR calculated from band shift distances for EMSAs (Fig. S1J) and open blue circles and dotted lines are 1/normalised signal change for ELISA competition experiments (derived from (D) for comparison). For all experiments other than ELISAs, AtLa1 concentrations are divided by the fold increase in AtTR concentration. ( G ) MST experiments detecting AtTR-Cy5 in the presence of excess unlabelled competitor RNA as annotated (Table S4), AtTR-AtLa1 data are reproduced from (F) for comparison.

    Journal: bioRxiv

    Article Title: La protein binding to telomerase RNA supports an evolutionary relationship between plant and ciliate telomerase pathways

    doi: 10.64898/2026.01.19.700320

    Figure Lengend Snippet: ( A ) Domain organisation of La and LARP7 proteins ( , , ), Tetrahymena Mlp1 is based on Alphafold3 domain predictions and sequence alignments (Figure S5A) and includes an apparent additional xRRM in a region known to bind RNA . Domains are as annotated, ‘+’ or ‘-‘ indicates regions of the sequence with correspondingly charged residues at neutral pH. ( B ) AtLa1 EMSA using 1% agarose gel with 80 nM AtTR 1-268 and protein concentrations (nM) as annotated, visualized by fluorescent staining. ( C ) Representative AtLa1 EMSAs with pre-tsnoR43.1, pretsnoR43.1ΔU and snoR43.1 substrates ( , ), as annotated, conditions as (B). White lines have been added to separate panels from the same gel. ( D ) ELISA experiments detecting immunolabelled AtLa1 bound to ≤0.5 pmol biotinylated AtTR 1-268 and non-biotinylated competitor RNA as annotated, (ytRNA, budding yeast tRNA). Lines show equations fit to data used to calculate K D , average AtTR values are shown in all experiments for comparison, error bars are the standard deviation. ( E ) ELISA experiments as (D) with plant TR competitors (full details in Table S2). ( F ) Comparison of AtLa1-AtTR binding assays used in this work. Solid black circles are average initial capillary fluorescence values (upper panel) or 1.5 s T-jump data (lower panel) from MST experiments, signal is from 5 nM 3’ Cy5-labelled AtTR 1-268. Solid lines show equations fit to data used to calculate K D (Table S3), dotted lines for both fast processes are Hill equation fits with n=2 for comparison, error bars are standard deviation. Open black circles with dashed lines are normalised fluorescence emission at 680 nM from 20 nM AtTR-Cy5, with excitation at 625 nM using a traditional spectrofluorometer (full spectra in Fig. S1H). Closed red circles show normalised Δε at 265 nM from circular dichroism experiments monitoring 50 nM unlabelled AtTR (difference spectra in Fig. S1I). Blue closed circles are normalised fractional saturation of 40 nM unlabelled AtTR calculated from band shift distances for EMSAs (Fig. S1J) and open blue circles and dotted lines are 1/normalised signal change for ELISA competition experiments (derived from (D) for comparison). For all experiments other than ELISAs, AtLa1 concentrations are divided by the fold increase in AtTR concentration. ( G ) MST experiments detecting AtTR-Cy5 in the presence of excess unlabelled competitor RNA as annotated (Table S4), AtTR-AtLa1 data are reproduced from (F) for comparison.

    Article Snippet: For ELISA or MST experiments, synthesised RNA was 3’ labelled with biotin- or Cy5-labelled cytosine bisphosphate, respectively (Thermo Scientific #20160, Jena Biosciences #NU-1706-CY5), using PierceTM RNA 3’ End Biotinylation Kit (Thermo Scientific, #20160) according to the manufacturer’s instructions.

    Techniques: Sequencing, Agarose Gel Electrophoresis, Staining, Enzyme-linked Immunosorbent Assay, Comparison, Standard Deviation, Binding Assay, Fluorescence, Circular Dichroism, Electrophoretic Mobility Shift Assay, Derivative Assay, Concentration Assay

    ( A,D ) Initial capillary fluorescence values from MST experiments for 5 nM 3’ Cy5-labelled AtTR 1-268 and (A) AtTERT minimal binding domain (TRBD) or (D) AtDomino, with or without constant AtLa1 as annotated. AtDomino average data are reproduced from , TRBD average data are reproduced from Figure S4E. Lines show fittings used to calculate K D values, error bars represent standard deviation. ( B ) Multicomponent yeast three-hybrid experiments pairing AtTR 1-268 MS2 or MS2 only with AD constructs of AtTERT TRBD variants in the presence of AtLa1 BD or empty BD constructs, as annotated. Numbers refer to mM concentrations of 3-aminotriazole in growth media, letters refer to amino acids absent for growth. ( C,F ) Schemas of (C) partial AtTERT-TR-La1 complex omitting AtTERT TEN, RT and CTE domains, (F) possible AtTR-La1-Domino complex, with domains as annotated, LaM in grey, xRRM in red, DUF3223 in yellow, TRBD in pink and RNA-binding linker in cyan. ( E ) Mass photometry (MP) deconvoluted mass spectra of samples with AtLa1, AtLa1+AtDomino with or without AtTR, as annotated, Solid lines show Gaussian fittings with values in text, annotated with average mass values in kDa, numbers in grey are peaks which cannot be unambiguously assigned (more details in Table S5).

    Journal: bioRxiv

    Article Title: La protein binding to telomerase RNA supports an evolutionary relationship between plant and ciliate telomerase pathways

    doi: 10.64898/2026.01.19.700320

    Figure Lengend Snippet: ( A,D ) Initial capillary fluorescence values from MST experiments for 5 nM 3’ Cy5-labelled AtTR 1-268 and (A) AtTERT minimal binding domain (TRBD) or (D) AtDomino, with or without constant AtLa1 as annotated. AtDomino average data are reproduced from , TRBD average data are reproduced from Figure S4E. Lines show fittings used to calculate K D values, error bars represent standard deviation. ( B ) Multicomponent yeast three-hybrid experiments pairing AtTR 1-268 MS2 or MS2 only with AD constructs of AtTERT TRBD variants in the presence of AtLa1 BD or empty BD constructs, as annotated. Numbers refer to mM concentrations of 3-aminotriazole in growth media, letters refer to amino acids absent for growth. ( C,F ) Schemas of (C) partial AtTERT-TR-La1 complex omitting AtTERT TEN, RT and CTE domains, (F) possible AtTR-La1-Domino complex, with domains as annotated, LaM in grey, xRRM in red, DUF3223 in yellow, TRBD in pink and RNA-binding linker in cyan. ( E ) Mass photometry (MP) deconvoluted mass spectra of samples with AtLa1, AtLa1+AtDomino with or without AtTR, as annotated, Solid lines show Gaussian fittings with values in text, annotated with average mass values in kDa, numbers in grey are peaks which cannot be unambiguously assigned (more details in Table S5).

    Article Snippet: For ELISA or MST experiments, synthesised RNA was 3’ labelled with biotin- or Cy5-labelled cytosine bisphosphate, respectively (Thermo Scientific #20160, Jena Biosciences #NU-1706-CY5), using PierceTM RNA 3’ End Biotinylation Kit (Thermo Scientific, #20160) according to the manufacturer’s instructions.

    Techniques: Fluorescence, Binding Assay, Standard Deviation, Construct, RNA Binding Assay

    ( A ) Domain structure of AtLa1, including LaM (grey) and xRRM (red), as predicted by Alphafold2 , and visualized using ChimeraX . xRRM residues chosen for mutagenesis studies are shown in a magnified panel (the same colour scheme is used in B-E). ( B-E ) Binding of AtLa1 fragments (B, C) and AtLa1 xRRM point variants (D, E) to AtTR investigated by EMSA (B, D) and MST (C, E). (B, D) Representative band shift of 80 nM AtTR 1-268 caused by binding of AtLa1 protein constructs (concentrations in nM) is visualised in agarose gel by fluorescent staining. White lines have been added to separate panels in the same gel (full image in Figure S2). (C, E) Initial capillary fluorescence values from MST experiments (upper panels) or MST 1.5 s T-jump data (lower panels) for 3’ Cy5-labelled AtTR 1-268 and La1 fragments as indicated, with average AtLa1 FL data from reproduced for comparison. Open symbols and dashed lines in (C), lower panel only, show data in the presence of 100x excess unlabelled tRNA competitor. Lines show equations fit to data used to calculate K D , error bars are the standard deviation.

    Journal: bioRxiv

    Article Title: La protein binding to telomerase RNA supports an evolutionary relationship between plant and ciliate telomerase pathways

    doi: 10.64898/2026.01.19.700320

    Figure Lengend Snippet: ( A ) Domain structure of AtLa1, including LaM (grey) and xRRM (red), as predicted by Alphafold2 , and visualized using ChimeraX . xRRM residues chosen for mutagenesis studies are shown in a magnified panel (the same colour scheme is used in B-E). ( B-E ) Binding of AtLa1 fragments (B, C) and AtLa1 xRRM point variants (D, E) to AtTR investigated by EMSA (B, D) and MST (C, E). (B, D) Representative band shift of 80 nM AtTR 1-268 caused by binding of AtLa1 protein constructs (concentrations in nM) is visualised in agarose gel by fluorescent staining. White lines have been added to separate panels in the same gel (full image in Figure S2). (C, E) Initial capillary fluorescence values from MST experiments (upper panels) or MST 1.5 s T-jump data (lower panels) for 3’ Cy5-labelled AtTR 1-268 and La1 fragments as indicated, with average AtLa1 FL data from reproduced for comparison. Open symbols and dashed lines in (C), lower panel only, show data in the presence of 100x excess unlabelled tRNA competitor. Lines show equations fit to data used to calculate K D , error bars are the standard deviation.

    Article Snippet: For ELISA or MST experiments, synthesised RNA was 3’ labelled with biotin- or Cy5-labelled cytosine bisphosphate, respectively (Thermo Scientific #20160, Jena Biosciences #NU-1706-CY5), using PierceTM RNA 3’ End Biotinylation Kit (Thermo Scientific, #20160) according to the manufacturer’s instructions.

    Techniques: Mutagenesis, Binding Assay, Electrophoretic Mobility Shift Assay, Construct, Agarose Gel Electrophoresis, Staining, Fluorescence, Comparison, Standard Deviation

    ( A ) Overview and legend of representative AtTR constructs used in La1 binding experiments (B-E, additional constructs in Figure S6A), template (cyan) and deleted P4 (red) region are highlighted. ( B ) ELISA competition experiments detecting immunolabelled AtLa1 bound to ≤0.5 pmol biotinylated AtTR 1-268 and non-biotinylated competitor AtTR fragments. ( C, D, E ) Initial capillary fluorescence values from MST experiments (upper panel) or MST 1.5 s T-jump data (lower panel) for 5 nM 3’ Cy5-labelled AtTR fragments and La1 FL (C), LaM (D) or xRRM (E). Lines show equations fit to data used to calculate K D . ( F ) Schema of AtTR regions which bind AtLa1 LaM (grey) or xRRM (red) domains. Possible binding sites are shown in black, unlikely/nonspecific binding sites in light grey. ( G ) K D values from AtLa1 ELISA competition experiments as (B) but with varying AtTR 3’ termini. The line shows fitting to a Gaussian distribution centred on 275 nt, full details in Figure S3B-C.

    Journal: bioRxiv

    Article Title: La protein binding to telomerase RNA supports an evolutionary relationship between plant and ciliate telomerase pathways

    doi: 10.64898/2026.01.19.700320

    Figure Lengend Snippet: ( A ) Overview and legend of representative AtTR constructs used in La1 binding experiments (B-E, additional constructs in Figure S6A), template (cyan) and deleted P4 (red) region are highlighted. ( B ) ELISA competition experiments detecting immunolabelled AtLa1 bound to ≤0.5 pmol biotinylated AtTR 1-268 and non-biotinylated competitor AtTR fragments. ( C, D, E ) Initial capillary fluorescence values from MST experiments (upper panel) or MST 1.5 s T-jump data (lower panel) for 5 nM 3’ Cy5-labelled AtTR fragments and La1 FL (C), LaM (D) or xRRM (E). Lines show equations fit to data used to calculate K D . ( F ) Schema of AtTR regions which bind AtLa1 LaM (grey) or xRRM (red) domains. Possible binding sites are shown in black, unlikely/nonspecific binding sites in light grey. ( G ) K D values from AtLa1 ELISA competition experiments as (B) but with varying AtTR 3’ termini. The line shows fitting to a Gaussian distribution centred on 275 nt, full details in Figure S3B-C.

    Article Snippet: For ELISA or MST experiments, synthesised RNA was 3’ labelled with biotin- or Cy5-labelled cytosine bisphosphate, respectively (Thermo Scientific #20160, Jena Biosciences #NU-1706-CY5), using PierceTM RNA 3’ End Biotinylation Kit (Thermo Scientific, #20160) according to the manufacturer’s instructions.

    Techniques: Construct, Binding Assay, Enzyme-linked Immunosorbent Assay, Fluorescence

    ( A ) Alphafold3 prediction of AtLa1-AtDomino complex showing AtLa1 LaM (La motif and RRM, grey) and xRRM (red), and AtDomino DUF3223 (yellow) domains. Highlighted panel shows interacting AtLa1 residues (green) on the RRM-DUF3223 interface. Structural visualisations prepared using ChimeraX . ( B ) Yeast 2-hybrid and ( C ) semi-quantitative beta galactosidase assays pairing Gal4 binding domain (BD) fused AtLa1 fragments and variants with Gal4 activation domain (AD) fused AtDomino. For (B), numbers refer to mM concentrations of 3-aminotriazole in the growth media, letters refer to amino acids absent for growth. For (C), BD-fused AtLa1 (purple bars) are compared to empty BD (grey bars), error bars represent standard deviation. ( D ) In vitro ELISA detecting AtDomino bound to immobilised AtLa1 WT (black circles) and AtLa1 SYD124GGG (dark red stars). Lines show equations fit to data used to calculate K D . ( E ) Domain structure of AtLa1 and AtDomino showing protein-protein (black arrows) and protein-RNA interactions (green bars), predicted domains as annotated, ‘+’ or ‘-‘ indicates regions of the sequence with correspondingly charged residues at neutral pH. ( F ) Initial capillary fluorescence values (left) and MST 1.5 s T-jump data (right) for AtDomino (black diamonds) and AtDomino delC (green diamonds) with 5 nM 3’ Cy5-labelled AtTR 1-268. For comparison, AtDomino interaction with Cy5-AtTR in the presence of excess unlabelled ytRNA competitor (open black diamonds, dashed lines) is shown. Lines show equations fit to data used to calculate K D , error bars represent standard deviation.

    Journal: bioRxiv

    Article Title: La protein binding to telomerase RNA supports an evolutionary relationship between plant and ciliate telomerase pathways

    doi: 10.64898/2026.01.19.700320

    Figure Lengend Snippet: ( A ) Alphafold3 prediction of AtLa1-AtDomino complex showing AtLa1 LaM (La motif and RRM, grey) and xRRM (red), and AtDomino DUF3223 (yellow) domains. Highlighted panel shows interacting AtLa1 residues (green) on the RRM-DUF3223 interface. Structural visualisations prepared using ChimeraX . ( B ) Yeast 2-hybrid and ( C ) semi-quantitative beta galactosidase assays pairing Gal4 binding domain (BD) fused AtLa1 fragments and variants with Gal4 activation domain (AD) fused AtDomino. For (B), numbers refer to mM concentrations of 3-aminotriazole in the growth media, letters refer to amino acids absent for growth. For (C), BD-fused AtLa1 (purple bars) are compared to empty BD (grey bars), error bars represent standard deviation. ( D ) In vitro ELISA detecting AtDomino bound to immobilised AtLa1 WT (black circles) and AtLa1 SYD124GGG (dark red stars). Lines show equations fit to data used to calculate K D . ( E ) Domain structure of AtLa1 and AtDomino showing protein-protein (black arrows) and protein-RNA interactions (green bars), predicted domains as annotated, ‘+’ or ‘-‘ indicates regions of the sequence with correspondingly charged residues at neutral pH. ( F ) Initial capillary fluorescence values (left) and MST 1.5 s T-jump data (right) for AtDomino (black diamonds) and AtDomino delC (green diamonds) with 5 nM 3’ Cy5-labelled AtTR 1-268. For comparison, AtDomino interaction with Cy5-AtTR in the presence of excess unlabelled ytRNA competitor (open black diamonds, dashed lines) is shown. Lines show equations fit to data used to calculate K D , error bars represent standard deviation.

    Article Snippet: For ELISA or MST experiments, synthesised RNA was 3’ labelled with biotin- or Cy5-labelled cytosine bisphosphate, respectively (Thermo Scientific #20160, Jena Biosciences #NU-1706-CY5), using PierceTM RNA 3’ End Biotinylation Kit (Thermo Scientific, #20160) according to the manufacturer’s instructions.

    Techniques: Binding Assay, Activation Assay, Standard Deviation, In Vitro, Enzyme-linked Immunosorbent Assay, Sequencing, Fluorescence, Comparison