| Project/Area Number |
06454672
|
|---|
| Research Category |
Grant-in-Aid for General Scientific Research (B)
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
Molecular biology
|
|---|
| Research Institution | National Institute of Genetics |
|---|
Principal Investigator |
ISHIHAMA Akira National Institute of Genetics, Department of Molecular Genetics, Professor, 分子遺伝研究系, 教授 (80019869)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
FUJITA Nobuyuki National Institute of Genetics, Department of Molecular Genetics, Assistant Prof, 分子遺伝研究系, 助手 (90173434)
|
|---|
| Project Period (FY) |
1994 – 1995
|
| Keywords | RNA polymerase / Transcription factor / Transcription regulation / Molecular assembly / Protein structure / Transcription signal / Protein-protein communication |
|---|
| Research Abstract |
RNA polymerase with the catalytic activity of RNA synthesis plays a Key role in gene transcription. Swiching of the global pattern of transcription takes place by modulating the promoter selectivity of RNA polymerase after interaction with various trans-acting protein and nucleotide factors. In order to understand the molecular mechaninism of promoter selectivity control of RNA polymerase, we have carried out a systematic mapping of the transcription factor contact sites on RNA polymerase. For this purpose, we reconstituted mutant E.coli RNA polymerases consisting of deletion, insertion or amino acid substitution mutant subunits and examined their responses to various transcription factors. Results indicated that : (i) the molecular contact between RNA polymerase and transcription factors involves narrow regions of about 10 amino acid residues on each component ; (ii) the contact sites are clustered on a short segment of each subunit, i.e., class-I factors on the C-terminal domain of alpha subunit and class-II factors on the C-terminal domain of sigma subunit ; and (iii) both protein factors and DNA enhancer signals interact with the same protein surface of RNA polymerase subunits as analyzed by NMR.The same line of studies has been initiated for mapping of protein-protein contact sites on RNA polymerase II from fission yeast S.pombe and on RNA polymerase from influenza viruses.
|
