Yeast RAD3 Protein Binds Directly to Both SSL2 and SSL1 Proteins: Implications for the Structure and Function of Transcription/Repair Factor b
The RAD3 and SSL2 gene products are essential proteins that are also required for the nucleotide excision repair pathway. We have recently demonstrated that the RAD3 gene product along with the SSL1 and TFB1 gene products are subunits of RNA polymerase II basal transcription factor b. Additionally,...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1994-04, Vol.91 (9), p.3926-3930 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Bardwell, Lee Bardwell, A. Jane Feaver, W. John Svejstrup, Jesper Q. Kornberg, Roger D. Friedberg, Errol C. |
| description | The RAD3 and SSL2 gene products are essential proteins that are also required for the nucleotide excision repair pathway. We have recently demonstrated that the RAD3 gene product along with the SSL1 and TFB1 gene products are subunits of RNA polymerase II basal transcription factor b. Additionally, the SSL2 gene product physically interacts with purified factor b. Here we combine an in vitro immunoprecipitation assay and an in vivo genetic assay to demonstrate a series of pairwise protein-protein interactions involving these components. RAD3 protein binds directly to both SSL2 protein and SSL1 protein in vitro. SSL1 protein interacts with itself and with RAD3 and TFB1 proteins in living yeast cells. An N-terminal, possibly noncatalytic, domain of SSL2 protein is sufficient for the factor b-SSL2 interaction, and a product of a DNA repair-defective allele of SSL2 is not defective in binding to factor b. We present genetic evidence suggesting that the DNA-repair function of SSL2 protein is not dependent on its essential function. |
| doi_str_mv | 10.1073/pnas.91.9.3926 |
| format | Article |
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Jane ; Feaver, W. John ; Svejstrup, Jesper Q. ; Kornberg, Roger D. ; Friedberg, Errol C.</creator><creatorcontrib>Bardwell, Lee ; Bardwell, A. Jane ; Feaver, W. John ; Svejstrup, Jesper Q. ; Kornberg, Roger D. ; Friedberg, Errol C.</creatorcontrib><description>The RAD3 and SSL2 gene products are essential proteins that are also required for the nucleotide excision repair pathway. We have recently demonstrated that the RAD3 gene product along with the SSL1 and TFB1 gene products are subunits of RNA polymerase II basal transcription factor b. Additionally, the SSL2 gene product physically interacts with purified factor b. Here we combine an in vitro immunoprecipitation assay and an in vivo genetic assay to demonstrate a series of pairwise protein-protein interactions involving these components. RAD3 protein binds directly to both SSL2 protein and SSL1 protein in vitro. SSL1 protein interacts with itself and with RAD3 and TFB1 proteins in living yeast cells. An N-terminal, possibly noncatalytic, domain of SSL2 protein is sufficient for the factor b-SSL2 interaction, and a product of a DNA repair-defective allele of SSL2 is not defective in binding to factor b. We present genetic evidence suggesting that the DNA-repair function of SSL2 protein is not dependent on its essential function.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.91.9.3926</identifier><identifier>PMID: 8171014</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Adenosine Triphosphatases - metabolism ; Alleles ; Base Sequence ; Biochemistry ; Biological and medical sciences ; Deoxyribonucleic acid ; DNA ; DNA Helicases - metabolism ; DNA Primers - chemistry ; DNA Repair ; DNA-Binding Proteins - metabolism ; Fundamental and applied biological sciences. Psychology ; Fungal Proteins - metabolism ; Genes ; Immunoprecipitation ; Macromolecular Substances ; Mathematical functions ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; Plasmids ; Protein Binding ; Proteins ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins ; Structure-Activity Relationship ; Transcription Factor TFIIH ; Transcription Factors - metabolism ; Transcription Factors, TFII ; Transcription, Genetic ; Transcription. Transcription factor. Splicing. 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Jane</creatorcontrib><creatorcontrib>Feaver, W. John</creatorcontrib><creatorcontrib>Svejstrup, Jesper Q.</creatorcontrib><creatorcontrib>Kornberg, Roger D.</creatorcontrib><creatorcontrib>Friedberg, Errol C.</creatorcontrib><title>Yeast RAD3 Protein Binds Directly to Both SSL2 and SSL1 Proteins: Implications for the Structure and Function of Transcription/Repair Factor b</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The RAD3 and SSL2 gene products are essential proteins that are also required for the nucleotide excision repair pathway. We have recently demonstrated that the RAD3 gene product along with the SSL1 and TFB1 gene products are subunits of RNA polymerase II basal transcription factor b. Additionally, the SSL2 gene product physically interacts with purified factor b. Here we combine an in vitro immunoprecipitation assay and an in vivo genetic assay to demonstrate a series of pairwise protein-protein interactions involving these components. RAD3 protein binds directly to both SSL2 protein and SSL1 protein in vitro. SSL1 protein interacts with itself and with RAD3 and TFB1 proteins in living yeast cells. An N-terminal, possibly noncatalytic, domain of SSL2 protein is sufficient for the factor b-SSL2 interaction, and a product of a DNA repair-defective allele of SSL2 is not defective in binding to factor b. We present genetic evidence suggesting that the DNA-repair function of SSL2 protein is not dependent on its essential function.</description><subject>Adenosine Triphosphatases - metabolism</subject><subject>Alleles</subject><subject>Base Sequence</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA Helicases - metabolism</subject><subject>DNA Primers - chemistry</subject><subject>DNA Repair</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal Proteins - metabolism</subject><subject>Genes</subject><subject>Immunoprecipitation</subject><subject>Macromolecular Substances</subject><subject>Mathematical functions</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Plasmids</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Structure-Activity Relationship</subject><subject>Transcription Factor TFIIH</subject><subject>Transcription Factors - metabolism</subject><subject>Transcription Factors, TFII</subject><subject>Transcription, Genetic</subject><subject>Transcription. Transcription factor. Splicing. 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Jane ; Feaver, W. John ; Svejstrup, Jesper Q. ; Kornberg, Roger D. ; Friedberg, Errol C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4596-247c281a35889d9abe6427bb1de5427be9555dc16153e2686c1cfbf111514d353</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Adenosine Triphosphatases - metabolism</topic><topic>Alleles</topic><topic>Base Sequence</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA Helicases - metabolism</topic><topic>DNA Primers - chemistry</topic><topic>DNA Repair</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal Proteins - metabolism</topic><topic>Genes</topic><topic>Immunoprecipitation</topic><topic>Macromolecular Substances</topic><topic>Mathematical functions</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>Plasmids</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Structure-Activity Relationship</topic><topic>Transcription Factor TFIIH</topic><topic>Transcription Factors - metabolism</topic><topic>Transcription Factors, TFII</topic><topic>Transcription, Genetic</topic><topic>Transcription. Transcription factor. Splicing. Rna processing</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bardwell, Lee</creatorcontrib><creatorcontrib>Bardwell, A. Jane</creatorcontrib><creatorcontrib>Feaver, W. 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Jane</au><au>Feaver, W. John</au><au>Svejstrup, Jesper Q.</au><au>Kornberg, Roger D.</au><au>Friedberg, Errol C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Yeast RAD3 Protein Binds Directly to Both SSL2 and SSL1 Proteins: Implications for the Structure and Function of Transcription/Repair Factor b</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1994-04-26</date><risdate>1994</risdate><volume>91</volume><issue>9</issue><spage>3926</spage><epage>3930</epage><pages>3926-3930</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>The RAD3 and SSL2 gene products are essential proteins that are also required for the nucleotide excision repair pathway. We have recently demonstrated that the RAD3 gene product along with the SSL1 and TFB1 gene products are subunits of RNA polymerase II basal transcription factor b. Additionally, the SSL2 gene product physically interacts with purified factor b. Here we combine an in vitro immunoprecipitation assay and an in vivo genetic assay to demonstrate a series of pairwise protein-protein interactions involving these components. RAD3 protein binds directly to both SSL2 protein and SSL1 protein in vitro. SSL1 protein interacts with itself and with RAD3 and TFB1 proteins in living yeast cells. An N-terminal, possibly noncatalytic, domain of SSL2 protein is sufficient for the factor b-SSL2 interaction, and a product of a DNA repair-defective allele of SSL2 is not defective in binding to factor b. We present genetic evidence suggesting that the DNA-repair function of SSL2 protein is not dependent on its essential function.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>8171014</pmid><doi>10.1073/pnas.91.9.3926</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1994-04, Vol.91 (9), p.3926-3930 |
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| recordid | cdi_pubmed_primary_8171014 |
| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Adenosine Triphosphatases - metabolism Alleles Base Sequence Biochemistry Biological and medical sciences Deoxyribonucleic acid DNA DNA Helicases - metabolism DNA Primers - chemistry DNA Repair DNA-Binding Proteins - metabolism Fundamental and applied biological sciences. Psychology Fungal Proteins - metabolism Genes Immunoprecipitation Macromolecular Substances Mathematical functions Molecular and cellular biology Molecular genetics Molecular Sequence Data Plasmids Protein Binding Proteins Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Structure-Activity Relationship Transcription Factor TFIIH Transcription Factors - metabolism Transcription Factors, TFII Transcription, Genetic Transcription. Transcription factor. Splicing. Rna processing Yeast Yeasts |
| title | Yeast RAD3 Protein Binds Directly to Both SSL2 and SSL1 Proteins: Implications for the Structure and Function of Transcription/Repair Factor b |
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