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poly(a) tract mrna isolation system iv  (Promega)

 
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    Promega poly(a) tract mrna isolation system iv
    Poly(a) Tract Mrna Isolation System Iv, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/poly+a++tract+isolation+system+iv/polyatract+mrna+isolation+system/pm20195770-65-20-26
    Average 90 stars, based on 1 article reviews
    poly(a) tract mrna isolation system iv - by Bioz Stars, 2026-09
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    other:

    Article Title: Expressed sequence tags-based identification of genes in a biocontrol strain Trichoderma asperellum.
    Article Snippet: Trichoderma asperellum, a filamentous soil fungus, is an effective biocontrol agent against many fungal plant pathogenic species.. In the present study, we investigated the biological control properties of the strain T. asperellum T4.. T. asperellum fermentation products significantly decreased the ability of Rhizoctonia solani and Sclerotinia sclerotiorum to infect rice and soybean, respectively.

    Article Title: A Functional Interface at the rDNA Connects rRNA Synthesis, Pre-rRNA Processing and Nucleolar Surveillance in Budding Yeast
    Article Snippet: Poly(A) + RNA purification used 500 μg of total RNAs and the Poly(A)tract mRNA isolation system IV (Promega).

    Article Title: Molecular cloning and functional analysis of Chinese sturgeon (Acipenser sinensis) growth hormone receptor.
    Article Snippet: A full length cDNA encoding the growth hormone receptor (GHR) of Chinese sturgeon was cloned in order to investigate the mechanism of growth hormone in regulating the growth of Chinese sturgeon.. The open reading frame of the cloned Chinese sturgeon growth hormone receptor (csGHR) cDNA encodes a trans-membrane protein of 611 amino acids containing all the characteristic motifs of GHR.. By sequence alignment, substitutions of amino acid residues highly conserved in other species were identified.

    Purification:

    Article Title: Exploring miRNAs involved in blue/UV-A light response in Brassica rapa reveals special regulatory mode during seedling development
    Article Snippet: .. Total RNA (3 μg) from light-treated seedlings was mixed equally and purified using PolyA Tract mRNA Isolation System IV (Promega, Madison, WI, USA), according to the manufacturer’s instructions. .. The 5′-Full RACE Kit (TaKaRa, Dalian, China) was used without the alkaline phosphatase and tobacco acid pyrophosphatase steps to detect the cleavage sites of the miRNA-targeted genes.

    Isolation:

    Article Title: Exploring miRNAs involved in blue/UV-A light response in Brassica rapa reveals special regulatory mode during seedling development
    Article Snippet: .. Total RNA (3 μg) from light-treated seedlings was mixed equally and purified using PolyA Tract mRNA Isolation System IV (Promega, Madison, WI, USA), according to the manufacturer’s instructions. .. The 5′-Full RACE Kit (TaKaRa, Dalian, China) was used without the alkaline phosphatase and tobacco acid pyrophosphatase steps to detect the cleavage sites of the miRNA-targeted genes.

    Article Title: A novel mutation from gene splicing of a voltage-gated sodium channel in a marine copepod and its potential effect on channel function
    Article Snippet: ⁎ Corresponding author.. Tel.. : +1 860 4059098.

    Article Title: Human proteins that specifically bind to 8-oxoguanine-containing RNA and their responses to oxidative stress.
    Article Snippet: Exposure of cells to oxygen radicals damage various biologically important molecules.. Among the oxidized bases produced in nucleic acids, 8-oxo-7,8-dihydroguanine (8-oxoguanine) is particularly important since it causes base mispairing.. To ensure accurate gene expression, organisms must have a mechanism to discriminate 8-oxoguanine-containing RNA from normal transcripts.

    Article Title: The nuclear RNA polymerase II surveillance system targets polymerase III transcripts
    Article Snippet: .. Poly(A) + RNA was prepared using PolyA tract mRNA isolation System IV (Promega) as amended by . ..

    Incubation:

    Article Title: Human proteins that specifically bind to 8-oxoguanine-containing RNA and their responses to oxidative stress.
    Article Snippet: Exposure of cells to oxygen radicals damage various biologically important molecules.. Among the oxidized bases produced in nucleic acids, 8-oxo-7,8-dihydroguanine (8-oxoguanine) is particularly important since it causes base mispairing.. To ensure accurate gene expression, organisms must have a mechanism to discriminate 8-oxoguanine-containing RNA from normal transcripts.

    Nucleic Acid Electrophoresis:

    Article Title: Human proteins that specifically bind to 8-oxoguanine-containing RNA and their responses to oxidative stress.
    Article Snippet: Exposure of cells to oxygen radicals damage various biologically important molecules.. Among the oxidized bases produced in nucleic acids, 8-oxo-7,8-dihydroguanine (8-oxoguanine) is particularly important since it causes base mispairing.. To ensure accurate gene expression, organisms must have a mechanism to discriminate 8-oxoguanine-containing RNA from normal transcripts.

    Binding Assay:

    Article Title: Human proteins that specifically bind to 8-oxoguanine-containing RNA and their responses to oxidative stress.
    Article Snippet: Exposure of cells to oxygen radicals damage various biologically important molecules.. Among the oxidized bases produced in nucleic acids, 8-oxo-7,8-dihydroguanine (8-oxoguanine) is particularly important since it causes base mispairing.. To ensure accurate gene expression, organisms must have a mechanism to discriminate 8-oxoguanine-containing RNA from normal transcripts.



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    poly(a) tract mrna isolation system iv  (Promega)
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    Promega poly(a) tract mrna isolation system iv
    Poly(a) Tract Mrna Isolation System Iv, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/poly+a++tract+isolation+system+iv/polyatract+mrna+isolation+system/pm20195770-65-20-26
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    poly(a)tract mrna isolation system iv  (Promega)
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    A , (left) Domain mapping of Nrd1. All three nrd1 alleles used in this work (provided by Prof. Jeff Corden, Johns Hopkins University School of Medicine) are HA-epitope tagged at the carboxyl terminal end of the protein, which allowed us to establish that neither mutation affects protein stability (see ). Nrd1 consists of an amino terminal RNA Pol II CTD interacting domain (CID), followed by a Nab3-interacting domain (Nab3), a central RE/RS-rich domain (RE/RS), an RNA binding domain (RRM), and a carboxyl terminal P/Q-rich-domain. The amino acid substitutions responsible for the thermosensitive phenotypes for growth in the conditional alleles, nrd1-101 and nrd1-102, are indicated. (right) Ten-fold serial dilutions of yeast cultures. Cells were grown on solid rich medium at the indicated temperatures for 2 d (30°C and 37°C) or 3 d (25°C). The Nrd1-HA-tagged wild-type control construct was fully functional. B, Analysis of the RRM mutation. (top) Northern-blot analysis of total and purified poly(A) + RNAs in different mutant background at the indicated temperatures. Poly(A) + RNA was purified on poly-dT-coated magnetic beads (see ). Total RNA and poly(A) + RNAs were loaded in a 1∶50 ratio, separated on 1.2% agarose/6% formaldehyde gel, transferred to nylon membranes and hybridized. Cells were grown to mid-log phase at 25°C and then transferred to the non-permissive temperature for 2 h. The probe used to detect the pre-rRNAs was LD471 (panel I, see ). Total RNA was normalized to SCR1. Poly(A) + RNA was normalized to the PGK1 <t>mRNA.</t> (bottom) Phosphor Imager quantitation. Histograms represent the relative distribution of specific RNA normalized to the PGK1 mRNA in different mutant background at different temperatures. C, Analysis of the CID mutation. Legend as in panel B. See also .
    Poly(a)tract Mrna Isolation System Iv, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    poly (a) tract mrna isolation system iv  (Promega)
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    A , (left) Domain mapping of Nrd1. All three nrd1 alleles used in this work (provided by Prof. Jeff Corden, Johns Hopkins University School of Medicine) are HA-epitope tagged at the carboxyl terminal end of the protein, which allowed us to establish that neither mutation affects protein stability (see ). Nrd1 consists of an amino terminal RNA Pol II CTD interacting domain (CID), followed by a Nab3-interacting domain (Nab3), a central RE/RS-rich domain (RE/RS), an RNA binding domain (RRM), and a carboxyl terminal P/Q-rich-domain. The amino acid substitutions responsible for the thermosensitive phenotypes for growth in the conditional alleles, nrd1-101 and nrd1-102, are indicated. (right) Ten-fold serial dilutions of yeast cultures. Cells were grown on solid rich medium at the indicated temperatures for 2 d (30°C and 37°C) or 3 d (25°C). The Nrd1-HA-tagged wild-type control construct was fully functional. B, Analysis of the RRM mutation. (top) Northern-blot analysis of total and purified poly(A) + RNAs in different mutant background at the indicated temperatures. Poly(A) + RNA was purified on poly-dT-coated magnetic beads (see ). Total RNA and poly(A) + RNAs were loaded in a 1∶50 ratio, separated on 1.2% agarose/6% formaldehyde gel, transferred to nylon membranes and hybridized. Cells were grown to mid-log phase at 25°C and then transferred to the non-permissive temperature for 2 h. The probe used to detect the pre-rRNAs was LD471 (panel I, see ). Total RNA was normalized to SCR1. Poly(A) + RNA was normalized to the PGK1 <t>mRNA.</t> (bottom) Phosphor Imager quantitation. Histograms represent the relative distribution of specific RNA normalized to the PGK1 mRNA in different mutant background at different temperatures. C, Analysis of the CID mutation. Legend as in panel B. See also .
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    poly a tract mrna isolation system iv  (Promega)
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    A , (left) Domain mapping of Nrd1. All three nrd1 alleles used in this work (provided by Prof. Jeff Corden, Johns Hopkins University School of Medicine) are HA-epitope tagged at the carboxyl terminal end of the protein, which allowed us to establish that neither mutation affects protein stability (see ). Nrd1 consists of an amino terminal RNA Pol II CTD interacting domain (CID), followed by a Nab3-interacting domain (Nab3), a central RE/RS-rich domain (RE/RS), an RNA binding domain (RRM), and a carboxyl terminal P/Q-rich-domain. The amino acid substitutions responsible for the thermosensitive phenotypes for growth in the conditional alleles, nrd1-101 and nrd1-102, are indicated. (right) Ten-fold serial dilutions of yeast cultures. Cells were grown on solid rich medium at the indicated temperatures for 2 d (30°C and 37°C) or 3 d (25°C). The Nrd1-HA-tagged wild-type control construct was fully functional. B, Analysis of the RRM mutation. (top) Northern-blot analysis of total and purified poly(A) + RNAs in different mutant background at the indicated temperatures. Poly(A) + RNA was purified on poly-dT-coated magnetic beads (see ). Total RNA and poly(A) + RNAs were loaded in a 1∶50 ratio, separated on 1.2% agarose/6% formaldehyde gel, transferred to nylon membranes and hybridized. Cells were grown to mid-log phase at 25°C and then transferred to the non-permissive temperature for 2 h. The probe used to detect the pre-rRNAs was LD471 (panel I, see ). Total RNA was normalized to SCR1. Poly(A) + RNA was normalized to the PGK1 <t>mRNA.</t> (bottom) Phosphor Imager quantitation. Histograms represent the relative distribution of specific RNA normalized to the PGK1 mRNA in different mutant background at different temperatures. C, Analysis of the CID mutation. Legend as in panel B. See also .
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    poly(a) tract mrna isolation system iv kit  (Promega)
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    A , (left) Domain mapping of Nrd1. All three nrd1 alleles used in this work (provided by Prof. Jeff Corden, Johns Hopkins University School of Medicine) are HA-epitope tagged at the carboxyl terminal end of the protein, which allowed us to establish that neither mutation affects protein stability (see ). Nrd1 consists of an amino terminal RNA Pol II CTD interacting domain (CID), followed by a Nab3-interacting domain (Nab3), a central RE/RS-rich domain (RE/RS), an RNA binding domain (RRM), and a carboxyl terminal P/Q-rich-domain. The amino acid substitutions responsible for the thermosensitive phenotypes for growth in the conditional alleles, nrd1-101 and nrd1-102, are indicated. (right) Ten-fold serial dilutions of yeast cultures. Cells were grown on solid rich medium at the indicated temperatures for 2 d (30°C and 37°C) or 3 d (25°C). The Nrd1-HA-tagged wild-type control construct was fully functional. B, Analysis of the RRM mutation. (top) Northern-blot analysis of total and purified poly(A) + RNAs in different mutant background at the indicated temperatures. Poly(A) + RNA was purified on poly-dT-coated magnetic beads (see ). Total RNA and poly(A) + RNAs were loaded in a 1∶50 ratio, separated on 1.2% agarose/6% formaldehyde gel, transferred to nylon membranes and hybridized. Cells were grown to mid-log phase at 25°C and then transferred to the non-permissive temperature for 2 h. The probe used to detect the pre-rRNAs was LD471 (panel I, see ). Total RNA was normalized to SCR1. Poly(A) + RNA was normalized to the PGK1 <t>mRNA.</t> (bottom) Phosphor Imager quantitation. Histograms represent the relative distribution of specific RNA normalized to the PGK1 mRNA in different mutant background at different temperatures. C, Analysis of the CID mutation. Legend as in panel B. See also .
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    polya tract poly(a)rna isolation system iv  (Promega)
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    A , (left) Domain mapping of Nrd1. All three nrd1 alleles used in this work (provided by Prof. Jeff Corden, Johns Hopkins University School of Medicine) are HA-epitope tagged at the carboxyl terminal end of the protein, which allowed us to establish that neither mutation affects protein stability (see ). Nrd1 consists of an amino terminal RNA Pol II CTD interacting domain (CID), followed by a Nab3-interacting domain (Nab3), a central RE/RS-rich domain (RE/RS), an RNA binding domain (RRM), and a carboxyl terminal P/Q-rich-domain. The amino acid substitutions responsible for the thermosensitive phenotypes for growth in the conditional alleles, nrd1-101 and nrd1-102, are indicated. (right) Ten-fold serial dilutions of yeast cultures. Cells were grown on solid rich medium at the indicated temperatures for 2 d (30°C and 37°C) or 3 d (25°C). The Nrd1-HA-tagged wild-type control construct was fully functional. B, Analysis of the RRM mutation. (top) Northern-blot analysis of total and purified poly(A) + RNAs in different mutant background at the indicated temperatures. Poly(A) + RNA was purified on poly-dT-coated magnetic beads (see ). Total RNA and poly(A) + RNAs were loaded in a 1∶50 ratio, separated on 1.2% agarose/6% formaldehyde gel, transferred to nylon membranes and hybridized. Cells were grown to mid-log phase at 25°C and then transferred to the non-permissive temperature for 2 h. The probe used to detect the pre-rRNAs was LD471 (panel I, see ). Total RNA was normalized to SCR1. Poly(A) + RNA was normalized to the PGK1 <t>mRNA.</t> (bottom) Phosphor Imager quantitation. Histograms represent the relative distribution of specific RNA normalized to the PGK1 mRNA in different mutant background at different temperatures. C, Analysis of the CID mutation. Legend as in panel B. See also .
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    poly a + tract mrna isolation system iv  (Promega)
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    A , (left) Domain mapping of Nrd1. All three nrd1 alleles used in this work (provided by Prof. Jeff Corden, Johns Hopkins University School of Medicine) are HA-epitope tagged at the carboxyl terminal end of the protein, which allowed us to establish that neither mutation affects protein stability (see ). Nrd1 consists of an amino terminal RNA Pol II CTD interacting domain (CID), followed by a Nab3-interacting domain (Nab3), a central RE/RS-rich domain (RE/RS), an RNA binding domain (RRM), and a carboxyl terminal P/Q-rich-domain. The amino acid substitutions responsible for the thermosensitive phenotypes for growth in the conditional alleles, nrd1-101 and nrd1-102, are indicated. (right) Ten-fold serial dilutions of yeast cultures. Cells were grown on solid rich medium at the indicated temperatures for 2 d (30°C and 37°C) or 3 d (25°C). The Nrd1-HA-tagged wild-type control construct was fully functional. B, Analysis of the RRM mutation. (top) Northern-blot analysis of total and purified poly(A) + RNAs in different mutant background at the indicated temperatures. Poly(A) + RNA was purified on poly-dT-coated magnetic beads (see ). Total RNA and poly(A) + RNAs were loaded in a 1∶50 ratio, separated on 1.2% agarose/6% formaldehyde gel, transferred to nylon membranes and hybridized. Cells were grown to mid-log phase at 25°C and then transferred to the non-permissive temperature for 2 h. The probe used to detect the pre-rRNAs was LD471 (panel I, see ). Total RNA was normalized to SCR1. Poly(A) + RNA was normalized to the PGK1 <t>mRNA.</t> (bottom) Phosphor Imager quantitation. Histograms represent the relative distribution of specific RNA normalized to the PGK1 mRNA in different mutant background at different temperatures. C, Analysis of the CID mutation. Legend as in panel B. See also .
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    A , (left) Domain mapping of Nrd1. All three nrd1 alleles used in this work (provided by Prof. Jeff Corden, Johns Hopkins University School of Medicine) are HA-epitope tagged at the carboxyl terminal end of the protein, which allowed us to establish that neither mutation affects protein stability (see ). Nrd1 consists of an amino terminal RNA Pol II CTD interacting domain (CID), followed by a Nab3-interacting domain (Nab3), a central RE/RS-rich domain (RE/RS), an RNA binding domain (RRM), and a carboxyl terminal P/Q-rich-domain. The amino acid substitutions responsible for the thermosensitive phenotypes for growth in the conditional alleles, nrd1-101 and nrd1-102, are indicated. (right) Ten-fold serial dilutions of yeast cultures. Cells were grown on solid rich medium at the indicated temperatures for 2 d (30°C and 37°C) or 3 d (25°C). The Nrd1-HA-tagged wild-type control construct was fully functional. B, Analysis of the RRM mutation. (top) Northern-blot analysis of total and purified poly(A) + RNAs in different mutant background at the indicated temperatures. Poly(A) + RNA was purified on poly-dT-coated magnetic beads (see ). Total RNA and poly(A) + RNAs were loaded in a 1∶50 ratio, separated on 1.2% agarose/6% formaldehyde gel, transferred to nylon membranes and hybridized. Cells were grown to mid-log phase at 25°C and then transferred to the non-permissive temperature for 2 h. The probe used to detect the pre-rRNAs was LD471 (panel I, see ). Total RNA was normalized to SCR1. Poly(A) + RNA was normalized to the PGK1 mRNA. (bottom) Phosphor Imager quantitation. Histograms represent the relative distribution of specific RNA normalized to the PGK1 mRNA in different mutant background at different temperatures. C, Analysis of the CID mutation. Legend as in panel B. See also .

    Journal: PLoS ONE

    Article Title: A Functional Interface at the rDNA Connects rRNA Synthesis, Pre-rRNA Processing and Nucleolar Surveillance in Budding Yeast

    doi: 10.1371/journal.pone.0024962

    Figure Lengend Snippet: A , (left) Domain mapping of Nrd1. All three nrd1 alleles used in this work (provided by Prof. Jeff Corden, Johns Hopkins University School of Medicine) are HA-epitope tagged at the carboxyl terminal end of the protein, which allowed us to establish that neither mutation affects protein stability (see ). Nrd1 consists of an amino terminal RNA Pol II CTD interacting domain (CID), followed by a Nab3-interacting domain (Nab3), a central RE/RS-rich domain (RE/RS), an RNA binding domain (RRM), and a carboxyl terminal P/Q-rich-domain. The amino acid substitutions responsible for the thermosensitive phenotypes for growth in the conditional alleles, nrd1-101 and nrd1-102, are indicated. (right) Ten-fold serial dilutions of yeast cultures. Cells were grown on solid rich medium at the indicated temperatures for 2 d (30°C and 37°C) or 3 d (25°C). The Nrd1-HA-tagged wild-type control construct was fully functional. B, Analysis of the RRM mutation. (top) Northern-blot analysis of total and purified poly(A) + RNAs in different mutant background at the indicated temperatures. Poly(A) + RNA was purified on poly-dT-coated magnetic beads (see ). Total RNA and poly(A) + RNAs were loaded in a 1∶50 ratio, separated on 1.2% agarose/6% formaldehyde gel, transferred to nylon membranes and hybridized. Cells were grown to mid-log phase at 25°C and then transferred to the non-permissive temperature for 2 h. The probe used to detect the pre-rRNAs was LD471 (panel I, see ). Total RNA was normalized to SCR1. Poly(A) + RNA was normalized to the PGK1 mRNA. (bottom) Phosphor Imager quantitation. Histograms represent the relative distribution of specific RNA normalized to the PGK1 mRNA in different mutant background at different temperatures. C, Analysis of the CID mutation. Legend as in panel B. See also .

    Article Snippet: Poly(A) + RNA purification used 500 μg of total RNAs and the Poly(A)tract mRNA isolation system IV (Promega).

    Techniques: Mutagenesis, RNA Binding Assay, Control, Construct, Functional Assay, Northern Blot, Purification, Magnetic Beads, Quantitation Assay

    A, (left) Domain mapping of Nab3. Nab3 consists of an amino terminal D/E-rich, a central RRM and a carboxyl terminal P/Q-rich domain. The two amino acid substitutions in the RRM domain responsible for the thermosensitive phenotypes in the nab3-11 are indicated (provided by Prof. Jeff Corden, Johns Hopkins University School of Medicine). (right) Ten-fold serial dilutions of yeast cultures. Cells were grown on solid rich medium at the indicated temperatures for 2 d (30°C and 37°C) or 3 d (25°C). B, Analysis of the Nab3 RRM mutation. (left) Northern-blot analysis of total and purified poly(A) + RNAs in different mutant background at the indicated temperatures (see legend to ). (right) Phosphor Imager quantitation. Histograms represent the relative distribution of specific RNA normalized to the PGK1 mRNA in different mutant background at different temperatures.

    Journal: PLoS ONE

    Article Title: A Functional Interface at the rDNA Connects rRNA Synthesis, Pre-rRNA Processing and Nucleolar Surveillance in Budding Yeast

    doi: 10.1371/journal.pone.0024962

    Figure Lengend Snippet: A, (left) Domain mapping of Nab3. Nab3 consists of an amino terminal D/E-rich, a central RRM and a carboxyl terminal P/Q-rich domain. The two amino acid substitutions in the RRM domain responsible for the thermosensitive phenotypes in the nab3-11 are indicated (provided by Prof. Jeff Corden, Johns Hopkins University School of Medicine). (right) Ten-fold serial dilutions of yeast cultures. Cells were grown on solid rich medium at the indicated temperatures for 2 d (30°C and 37°C) or 3 d (25°C). B, Analysis of the Nab3 RRM mutation. (left) Northern-blot analysis of total and purified poly(A) + RNAs in different mutant background at the indicated temperatures (see legend to ). (right) Phosphor Imager quantitation. Histograms represent the relative distribution of specific RNA normalized to the PGK1 mRNA in different mutant background at different temperatures.

    Article Snippet: Poly(A) + RNA purification used 500 μg of total RNAs and the Poly(A)tract mRNA isolation system IV (Promega).

    Techniques: Mutagenesis, Northern Blot, Purification, Quantitation Assay

    A, Spt4 and Spt5 interact functionally with Rrp6. Legend as in . B, RTqPCR analysis of the mRNA level of SPT5 (normalized to ACT1) in SPT5 DAmP at different temperature in the presence, and in the absence of Spt4 (n = 3). C, Pre-rRNA processing analysis. Total RNA was extracted from different mutants grown at the indicated temperature, separated on denaturing gels. Probes used to detect pre-rRNAs and rRNAs were: LD359 (panel I), LD339 (panel II), LD471 (panel III), LD1099 (panel IV), LD871 (panel V), and LD906 (panel VI); they are depicted in . Panel VI, as a control for detection of 6S and 5.8S+30, total RNA was extracted from ngl2 and rrp6 mutants, respectively. These precursors are so abundant in these mutants, that 10x less RNA was loaded in these lanes; consequently, these lanes show no signal for SCR1 on this exposure. This experiment was repeated three times and a representative case is shown. D, Spt4 is involved in nucleolar surveillance. (top) Northern-blot analysis of total and purified poly(A) + RNAs in different mutant background at 30°C (see legends to and ). (bottom) Phosphor Imager quantitation (see legends to and ).

    Journal: PLoS ONE

    Article Title: A Functional Interface at the rDNA Connects rRNA Synthesis, Pre-rRNA Processing and Nucleolar Surveillance in Budding Yeast

    doi: 10.1371/journal.pone.0024962

    Figure Lengend Snippet: A, Spt4 and Spt5 interact functionally with Rrp6. Legend as in . B, RTqPCR analysis of the mRNA level of SPT5 (normalized to ACT1) in SPT5 DAmP at different temperature in the presence, and in the absence of Spt4 (n = 3). C, Pre-rRNA processing analysis. Total RNA was extracted from different mutants grown at the indicated temperature, separated on denaturing gels. Probes used to detect pre-rRNAs and rRNAs were: LD359 (panel I), LD339 (panel II), LD471 (panel III), LD1099 (panel IV), LD871 (panel V), and LD906 (panel VI); they are depicted in . Panel VI, as a control for detection of 6S and 5.8S+30, total RNA was extracted from ngl2 and rrp6 mutants, respectively. These precursors are so abundant in these mutants, that 10x less RNA was loaded in these lanes; consequently, these lanes show no signal for SCR1 on this exposure. This experiment was repeated three times and a representative case is shown. D, Spt4 is involved in nucleolar surveillance. (top) Northern-blot analysis of total and purified poly(A) + RNAs in different mutant background at 30°C (see legends to and ). (bottom) Phosphor Imager quantitation (see legends to and ).

    Article Snippet: Poly(A) + RNA purification used 500 μg of total RNAs and the Poly(A)tract mRNA isolation system IV (Promega).

    Techniques: Control, Northern Blot, Purification, Mutagenesis, Quantitation Assay