Publication Date:
1994-10-21
Description:
RNA polymerases I, II, and III each use the TATA-binding protein (TBP). Regulators that target this shared factor may therefore provide a means to coordinate the activities of the three nuclear RNA polymerases. The repressor Dr1 binds to TBP and blocks the interaction of TBP with polymerase II- and polymerase III-specific factors. This enables Dr1 to coordinately regulate transcription by RNA polymerases II and III. Under the same conditions, Dr1 does not inhibit polymerase I transcription. By selectively repressing polymerases II and III, Dr1 may shift the physiological balance of transcriptional output in favor of polymerase I.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉White, R J -- Khoo, B C -- Inostroza, J A -- Reinberg, D -- Jackson, S P -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1994 Oct 21;266(5184):448-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome/CRC Institute, University of Cambridge, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939686" target="_blank"〉PubMed〈/a〉
Keywords:
Base Sequence
;
DNA-Binding Proteins/metabolism
;
HeLa Cells
;
Humans
;
Molecular Sequence Data
;
Phosphoproteins/metabolism/*pharmacology
;
RNA Polymerase I/*metabolism
;
RNA Polymerase II/*metabolism
;
RNA Polymerase III/*metabolism
;
Saccharomyces cerevisiae Proteins
;
TATA Box
;
TATA-Binding Protein Associated Factors
;
TATA-Box Binding Protein
;
Transcription Factor TFIIB
;
Transcription Factor TFIIIB
;
Transcription Factors/metabolism/*pharmacology
;
*Transcription Factors, TFIII
;
Transcription, Genetic/*drug effects
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
