PMID:11439189
| Citation |
Young, BA, Anthony, LC, Gruber, TM, Arthur, TM, Heyduk, E, Lu, CZ, Sharp, MM, Heyduk, T, Burgess, RR and Gross, CA (2001) A coiled-coil from the RNA polymerase beta' subunit allosterically induces selective nontemplate strand binding by sigma(70). Cell 105:935-44 |
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| Abstract |
For transcription to initiate, RNA polymerase must recognize and melt promoters. Selective binding to the nontemplate strand of the -10 region of the promoter is central to this process. We show that a 48 amino acid (aa) coiled-coil from the beta' subunit (aa 262--309) induces sigma(70) to perform this function almost as efficiently as core RNA polymerase itself. We provide evidence that interaction between the beta' coiled-coil and region 2.2 of sigma(70) promotes an allosteric transition that allows sigma(70) to selectively recognize the nontemplate strand. As the beta' 262--309 peptide can function with the previously crystallized portion of sigma(70), nontemplate recognition can be reconstituted with only 47 kDa, or 1/10 of holoenzyme. |
| Links | |
| Keywords |
Allosteric Regulation; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/genetics; DNA-Binding Proteins/metabolism; DNA-Directed RNA Polymerases/chemistry; DNA-Directed RNA Polymerases/genetics; DNA-Directed RNA Polymerases/metabolism; Models, Molecular; Mutation; Nucleic Acid Denaturation; Peptide Fragments/genetics; Peptide Fragments/metabolism; Promoter Regions, Genetic; Protein Structure, Tertiary; Sigma Factor/chemistry; Sigma Factor/metabolism; Transcription, Genetic |
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