Specific interaction between the nonphosphorylated form of RNA polymerase II and the TATA-binding protein
Fractionation of a transcription-competent HeLa cell extract on a column containing one copy of the heptamer repeat (YSPTSPS) present in the carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II resulted in the loss of transcriptional activity. Fractionation of the extracts on co...
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| Veröffentlicht in: | Cell 1992-05, Vol.69 (5), p.871-881 |
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| creator | Usheva, Anny Maldonado, Edio Goldring, Anat Lu, Hua Houbavi, Christo Reinberg, Danny Aloni, Yosef |
| description | Fractionation of a transcription-competent HeLa cell extract on a column containing one copy of the heptamer repeat (YSPTSPS) present in the carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II resulted in the loss of transcriptional activity. Fractionation of the extracts on columns containing mutations of the heptamer repeat was without effect. Such transcriptionally inactive extracts regained their ability to specifically transcribe different class II promoters upon the addition of human TFIID, recombinant yeast TATA-binding protein (TBP), or proteins bound to the column. Fractionation of RNA polymerase II on columns containing human or yeast TBP resulted in the specific retention of the nonphosphorylated form of RNA polymerase II. The phosphorylated form of the enzyme was unable to interact with TBP. The specific interaction of RNA polymerase II with TBP was mediated by the CTD of RNA polymerase II. |
| doi_str_mv | 10.1016/0092-8674(92)90297-P |
| format | Article |
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Fractionation of the extracts on columns containing mutations of the heptamer repeat was without effect. Such transcriptionally inactive extracts regained their ability to specifically transcribe different class II promoters upon the addition of human TFIID, recombinant yeast TATA-binding protein (TBP), or proteins bound to the column. Fractionation of RNA polymerase II on columns containing human or yeast TBP resulted in the specific retention of the nonphosphorylated form of RNA polymerase II. The phosphorylated form of the enzyme was unable to interact with TBP. The specific interaction of RNA polymerase II with TBP was mediated by the CTD of RNA polymerase II.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/0092-8674(92)90297-P</identifier><identifier>PMID: 1591781</identifier><identifier>CODEN: CELLB5</identifier><language>eng</language><publisher>Cambridge, MA: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Base Sequence ; Biological and medical sciences ; Blotting, Western ; Cell Extracts ; DNA-Binding Proteins - metabolism ; Fundamental and applied biological sciences. Psychology ; HeLa Cells ; Humans ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; Mutation - genetics ; Peptide Fragments - metabolism ; Phosphorylation ; Promoter Regions, Genetic - genetics ; Recombinant Proteins - metabolism ; Repetitive Sequences, Nucleic Acid - genetics ; RNA Polymerase II - metabolism ; TATA-Box Binding Protein ; Temperature ; Transcription Factor TFIID ; Transcription Factors - metabolism ; Transcription, Genetic - physiology ; Transcription. Transcription factor. Splicing. 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Fractionation of the extracts on columns containing mutations of the heptamer repeat was without effect. Such transcriptionally inactive extracts regained their ability to specifically transcribe different class II promoters upon the addition of human TFIID, recombinant yeast TATA-binding protein (TBP), or proteins bound to the column. Fractionation of RNA polymerase II on columns containing human or yeast TBP resulted in the specific retention of the nonphosphorylated form of RNA polymerase II. The phosphorylated form of the enzyme was unable to interact with TBP. The specific interaction of RNA polymerase II with TBP was mediated by the CTD of RNA polymerase II.</description><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Cell Extracts</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Mutation - genetics</subject><subject>Peptide Fragments - metabolism</subject><subject>Phosphorylation</subject><subject>Promoter Regions, Genetic - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Repetitive Sequences, Nucleic Acid - genetics</subject><subject>RNA Polymerase II - metabolism</subject><subject>TATA-Box Binding Protein</subject><subject>Temperature</subject><subject>Transcription Factor TFIID</subject><subject>Transcription Factors - metabolism</subject><subject>Transcription, Genetic - physiology</subject><subject>Transcription. Transcription factor. Splicing. 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Psychology</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>Mutation - genetics</topic><topic>Peptide Fragments - metabolism</topic><topic>Phosphorylation</topic><topic>Promoter Regions, Genetic - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Repetitive Sequences, Nucleic Acid - genetics</topic><topic>RNA Polymerase II - metabolism</topic><topic>TATA-Box Binding Protein</topic><topic>Temperature</topic><topic>Transcription Factor TFIID</topic><topic>Transcription Factors - metabolism</topic><topic>Transcription, Genetic - physiology</topic><topic>Transcription. Transcription factor. Splicing. Rna processing</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Usheva, Anny</creatorcontrib><creatorcontrib>Maldonado, Edio</creatorcontrib><creatorcontrib>Goldring, Anat</creatorcontrib><creatorcontrib>Lu, Hua</creatorcontrib><creatorcontrib>Houbavi, Christo</creatorcontrib><creatorcontrib>Reinberg, Danny</creatorcontrib><creatorcontrib>Aloni, Yosef</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Usheva, Anny</au><au>Maldonado, Edio</au><au>Goldring, Anat</au><au>Lu, Hua</au><au>Houbavi, Christo</au><au>Reinberg, Danny</au><au>Aloni, Yosef</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Specific interaction between the nonphosphorylated form of RNA polymerase II and the TATA-binding protein</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1992-05-29</date><risdate>1992</risdate><volume>69</volume><issue>5</issue><spage>871</spage><epage>881</epage><pages>871-881</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><coden>CELLB5</coden><abstract>Fractionation of a transcription-competent HeLa cell extract on a column containing one copy of the heptamer repeat (YSPTSPS) present in the carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II resulted in the loss of transcriptional activity. Fractionation of the extracts on columns containing mutations of the heptamer repeat was without effect. Such transcriptionally inactive extracts regained their ability to specifically transcribe different class II promoters upon the addition of human TFIID, recombinant yeast TATA-binding protein (TBP), or proteins bound to the column. Fractionation of RNA polymerase II on columns containing human or yeast TBP resulted in the specific retention of the nonphosphorylated form of RNA polymerase II. The phosphorylated form of the enzyme was unable to interact with TBP. The specific interaction of RNA polymerase II with TBP was mediated by the CTD of RNA polymerase II.</abstract><cop>Cambridge, MA</cop><pub>Elsevier Inc</pub><pmid>1591781</pmid><doi>10.1016/0092-8674(92)90297-P</doi><tpages>11</tpages></addata></record> |
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| subjects | Amino Acid Sequence Base Sequence Biological and medical sciences Blotting, Western Cell Extracts DNA-Binding Proteins - metabolism Fundamental and applied biological sciences. Psychology HeLa Cells Humans Molecular and cellular biology Molecular genetics Molecular Sequence Data Mutation - genetics Peptide Fragments - metabolism Phosphorylation Promoter Regions, Genetic - genetics Recombinant Proteins - metabolism Repetitive Sequences, Nucleic Acid - genetics RNA Polymerase II - metabolism TATA-Box Binding Protein Temperature Transcription Factor TFIID Transcription Factors - metabolism Transcription, Genetic - physiology Transcription. Transcription factor. Splicing. Rna processing |
| title | Specific interaction between the nonphosphorylated form of RNA polymerase II and the TATA-binding protein |
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