multiple sequence alignment for nucleotides and amino acid sequences bioedit 7.2 Search Results


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Identification and characterization of an LxLF motif from Rad5 and Rad18 . ( A ) Sequence alignment of the mapped minimum PCNA-binding regions in Rad5 and Rad18. The sequence alignment was performed by BioEdit 7.2. Residues highlighted in black are identical sequences and those in grey are conserved residues. ( B , C ) Physical interactions between Rad5/Rad18 and Pol30 by a Y2H assay. The 3A mutation indicates LxLF-to-AxAA amino acid substitution. Rad5 and Rad18 interactions with Smt3 served as positive controls, respectively. ( D ) Effects of 3A and 3E amino acid substitutions on the physical interaction between Rad5-N431 and Pol30 by a Y2H assay. The 3E mutation contains R187E, R229E, R241E triple substitutions; 3AE contains both 3A and 3E mutations. ( E , F) Assess physical interactions between Rad5 (177-348)/Rad18-N160 and Pol30 by a GST affinity pulldown assay. Experimental conditions were as described in Figure  B and  D. For the Y2H assay, at least two sets of independent transformants were tested with comparable results, and only one set of representative images is presented.
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Identification and characterization of an LxLF motif from Rad5 and Rad18 . ( A ) Sequence alignment of the mapped minimum PCNA-binding regions in Rad5 and Rad18. The sequence alignment was performed by BioEdit 7.2. Residues highlighted in black are identical sequences and those in grey are conserved residues. ( B , C ) Physical interactions between Rad5/Rad18 and Pol30 by a Y2H assay. The 3A mutation indicates LxLF-to-AxAA amino acid substitution. Rad5 and Rad18 interactions with Smt3 served as positive controls, respectively. ( D ) Effects of 3A and 3E amino acid substitutions on the physical interaction between Rad5-N431 and Pol30 by a Y2H assay. The 3E mutation contains R187E, R229E, R241E triple substitutions; 3AE contains both 3A and 3E mutations. ( E , F) Assess physical interactions between Rad5 (177-348)/Rad18-N160 and Pol30 by a GST affinity pulldown assay. Experimental conditions were as described in Figure  B and  D. For the Y2H assay, at least two sets of independent transformants were tested with comparable results, and only one set of representative images is presented.
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Identification and characterization of an LxLF motif from Rad5 and Rad18 . ( A ) Sequence alignment of the mapped minimum PCNA-binding regions in Rad5 and Rad18. The sequence alignment was performed by BioEdit 7.2. Residues highlighted in black are identical sequences and those in grey are conserved residues. ( B , C ) Physical interactions between Rad5/Rad18 and Pol30 by a Y2H assay. The 3A mutation indicates LxLF-to-AxAA amino acid substitution. Rad5 and Rad18 interactions with Smt3 served as positive controls, respectively. ( D ) Effects of 3A and 3E amino acid substitutions on the physical interaction between Rad5-N431 and Pol30 by a Y2H assay. The 3E mutation contains R187E, R229E, R241E triple substitutions; 3AE contains both 3A and 3E mutations. ( E , F) Assess physical interactions between Rad5 (177-348)/Rad18-N160 and Pol30 by a GST affinity pulldown assay. Experimental conditions were as described in Figure  B and  D. For the Y2H assay, at least two sets of independent transformants were tested with comparable results, and only one set of representative images is presented.
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Identification and characterization of an LxLF motif from Rad5 and Rad18 . ( A ) Sequence alignment of the mapped minimum PCNA-binding regions in Rad5 and Rad18. The sequence alignment was performed by BioEdit 7.2. Residues highlighted in black are identical sequences and those in grey are conserved residues. ( B , C ) Physical interactions between Rad5/Rad18 and Pol30 by a Y2H assay. The 3A mutation indicates LxLF-to-AxAA amino acid substitution. Rad5 and Rad18 interactions with Smt3 served as positive controls, respectively. ( D ) Effects of 3A and 3E amino acid substitutions on the physical interaction between Rad5-N431 and Pol30 by a Y2H assay. The 3E mutation contains R187E, R229E, R241E triple substitutions; 3AE contains both 3A and 3E mutations. ( E , F) Assess physical interactions between Rad5 (177-348)/Rad18-N160 and Pol30 by a GST affinity pulldown assay. Experimental conditions were as described in Figure  B and  D. For the Y2H assay, at least two sets of independent transformants were tested with comparable results, and only one set of representative images is presented.
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Identification and characterization of an LxLF motif from Rad5 and Rad18 . ( A ) Sequence alignment of the mapped minimum PCNA-binding regions in Rad5 and Rad18. The sequence alignment was performed by BioEdit 7.2. Residues highlighted in black are identical sequences and those in grey are conserved residues. ( B , C ) Physical interactions between Rad5/Rad18 and Pol30 by a Y2H assay. The 3A mutation indicates LxLF-to-AxAA amino acid substitution. Rad5 and Rad18 interactions with Smt3 served as positive controls, respectively. ( D ) Effects of 3A and 3E amino acid substitutions on the physical interaction between Rad5-N431 and Pol30 by a Y2H assay. The 3E mutation contains R187E, R229E, R241E triple substitutions; 3AE contains both 3A and 3E mutations. ( E , F) Assess physical interactions between Rad5 (177-348)/Rad18-N160 and Pol30 by a GST affinity pulldown assay. Experimental conditions were as described in Figure  B and  D. For the Y2H assay, at least two sets of independent transformants were tested with comparable results, and only one set of representative images is presented.
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Identification and characterization of an LxLF motif from Rad5 and Rad18 . ( A ) Sequence alignment of the mapped minimum PCNA-binding regions in Rad5 and Rad18. The sequence alignment was performed by BioEdit 7.2. Residues highlighted in black are identical sequences and those in grey are conserved residues. ( B , C ) Physical interactions between Rad5/Rad18 and Pol30 by a Y2H assay. The 3A mutation indicates LxLF-to-AxAA amino acid substitution. Rad5 and Rad18 interactions with Smt3 served as positive controls, respectively. ( D ) Effects of 3A and 3E amino acid substitutions on the physical interaction between Rad5-N431 and Pol30 by a Y2H assay. The 3E mutation contains R187E, R229E, R241E triple substitutions; 3AE contains both 3A and 3E mutations. ( E , F) Assess physical interactions between Rad5 (177-348)/Rad18-N160 and Pol30 by a GST affinity pulldown assay. Experimental conditions were as described in Figure  B and  D. For the Y2H assay, at least two sets of independent transformants were tested with comparable results, and only one set of representative images is presented.
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Identification and characterization of an LxLF motif from Rad5 and Rad18 . ( A ) Sequence alignment of the mapped minimum PCNA-binding regions in Rad5 and Rad18. The sequence alignment was performed by BioEdit 7.2. Residues highlighted in black are identical sequences and those in grey are conserved residues. ( B , C ) Physical interactions between Rad5/Rad18 and Pol30 by a Y2H assay. The 3A mutation indicates LxLF-to-AxAA amino acid substitution. Rad5 and Rad18 interactions with Smt3 served as positive controls, respectively. ( D ) Effects of 3A and 3E amino acid substitutions on the physical interaction between Rad5-N431 and Pol30 by a Y2H assay. The 3E mutation contains R187E, R229E, R241E triple substitutions; 3AE contains both 3A and 3E mutations. ( E , F) Assess physical interactions between Rad5 (177-348)/Rad18-N160 and Pol30 by a GST affinity pulldown assay. Experimental conditions were as described in Figure  B and  D. For the Y2H assay, at least two sets of independent transformants were tested with comparable results, and only one set of representative images is presented.
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Identification and characterization of an LxLF motif from Rad5 and Rad18 . ( A ) Sequence alignment of the mapped minimum PCNA-binding regions in Rad5 and Rad18. The sequence alignment was performed by BioEdit 7.2. Residues highlighted in black are identical sequences and those in grey are conserved residues. ( B , C ) Physical interactions between Rad5/Rad18 and Pol30 by a Y2H assay. The 3A mutation indicates LxLF-to-AxAA amino acid substitution. Rad5 and Rad18 interactions with Smt3 served as positive controls, respectively. ( D ) Effects of 3A and 3E amino acid substitutions on the physical interaction between Rad5-N431 and Pol30 by a Y2H assay. The 3E mutation contains R187E, R229E, R241E triple substitutions; 3AE contains both 3A and 3E mutations. ( E , F) Assess physical interactions between Rad5 (177-348)/Rad18-N160 and Pol30 by a GST affinity pulldown assay. Experimental conditions were as described in Figure  B and  D. For the Y2H assay, at least two sets of independent transformants were tested with comparable results, and only one set of representative images is presented.
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The mitochondrial genome of the Eurasian eagle-owl Bubo bubo (GenBank Accession No. OR756278 ). The <t>13</t> <t>protein-coding</t> <t>genes,</t> 23 tRNA, and <t>two</t> <t>rRNA</t> genes are shown in yellow, pink, and red, respectively.
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Image Search Results


Identification and characterization of an LxLF motif from Rad5 and Rad18 . ( A ) Sequence alignment of the mapped minimum PCNA-binding regions in Rad5 and Rad18. The sequence alignment was performed by BioEdit 7.2. Residues highlighted in black are identical sequences and those in grey are conserved residues. ( B , C ) Physical interactions between Rad5/Rad18 and Pol30 by a Y2H assay. The 3A mutation indicates LxLF-to-AxAA amino acid substitution. Rad5 and Rad18 interactions with Smt3 served as positive controls, respectively. ( D ) Effects of 3A and 3E amino acid substitutions on the physical interaction between Rad5-N431 and Pol30 by a Y2H assay. The 3E mutation contains R187E, R229E, R241E triple substitutions; 3AE contains both 3A and 3E mutations. ( E , F) Assess physical interactions between Rad5 (177-348)/Rad18-N160 and Pol30 by a GST affinity pulldown assay. Experimental conditions were as described in Figure  B and  D. For the Y2H assay, at least two sets of independent transformants were tested with comparable results, and only one set of representative images is presented.

Journal: International Journal of Biological Sciences

Article Title: Budding Yeast Ubiquitin Ligases Rad5 and Rad18 Bind a Novel PCNA Surface, which Is Required for their Functions in DNA-Damage Tolerance

doi: 10.7150/ijbs.124441

Figure Lengend Snippet: Identification and characterization of an LxLF motif from Rad5 and Rad18 . ( A ) Sequence alignment of the mapped minimum PCNA-binding regions in Rad5 and Rad18. The sequence alignment was performed by BioEdit 7.2. Residues highlighted in black are identical sequences and those in grey are conserved residues. ( B , C ) Physical interactions between Rad5/Rad18 and Pol30 by a Y2H assay. The 3A mutation indicates LxLF-to-AxAA amino acid substitution. Rad5 and Rad18 interactions with Smt3 served as positive controls, respectively. ( D ) Effects of 3A and 3E amino acid substitutions on the physical interaction between Rad5-N431 and Pol30 by a Y2H assay. The 3E mutation contains R187E, R229E, R241E triple substitutions; 3AE contains both 3A and 3E mutations. ( E , F) Assess physical interactions between Rad5 (177-348)/Rad18-N160 and Pol30 by a GST affinity pulldown assay. Experimental conditions were as described in Figure B and D. For the Y2H assay, at least two sets of independent transformants were tested with comparable results, and only one set of representative images is presented.

Article Snippet: Multiple alignments were performed and presented by BioEdit 7.2 ( https://bioedit.software.informer.com/7.2/ ).

Techniques: Sequencing, Binding Assay, Y2H Assay, Mutagenesis

The mitochondrial genome of the Eurasian eagle-owl Bubo bubo (GenBank Accession No. OR756278 ). The 13 protein-coding genes, 23 tRNA, and two rRNA genes are shown in yellow, pink, and red, respectively.

Journal: Mitochondrial DNA. Part B, Resources

Article Title: Complete mitochondrial genome sequence of the South Korean Eurasian eagle-owl, Bubo bubo spp. kiautschenis (Strigiformes; Strigidae)

doi: 10.1080/23802359.2025.2528345

Figure Lengend Snippet: The mitochondrial genome of the Eurasian eagle-owl Bubo bubo (GenBank Accession No. OR756278 ). The 13 protein-coding genes, 23 tRNA, and two rRNA genes are shown in yellow, pink, and red, respectively.

Article Snippet: The exact start-and-stop codons of all the protein-coding genes (PCGs) as well as the boundary of two ribosomal RNA (rRNA) genes were identified after aligning the newly analyzed complete mitochondrial sequence (in this study) with 19 other sequences (belonging to the Strigidae family retrieved from the GenBank database) using ClustalW multiple alignments in BioEdit v.7.2.

Techniques: