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HUMAN GENERAL TRANSCRIPTION FACTOR-IIH PHOSPHORYLATES THE C-TERMINAL DOMAIN OF RNA POLYMERASE-II
Author(s): LU H, ZAWEL L, FISHER L, EGLY JM, REINBERG D
Source: NATURE    Volume: 358    Issue: 6388    Pages: 641-645    Published: AUG 20 1992  
Times Cited: 292     References: 35     
Abstract: Phosphorylation of the carboxy-terminal domain of the largest subunit of RNA polymerase II is believed to control the transition from transcription initiation to elongation. The general transcription factor IIH (TFIIH) contains a kinase activity capable of phosphorylating this domain. Factors that promote the association of RNA polymerase II with the preinitiation complex stimulate this activity. The transcription factor IIE, which is required for the stable association of TFIIH with the preinitiation complex, affects the processivity of TFIIH kinase.
Document Type: Article
Language: English
Addresses:
1. UNIV MED & DENT NEW JERSEY, ROBERT WOOD JOHNSON MED SCH, DEPT BIOCHEM, 675 HOES LANE, PISCATAWAY, NJ 08854 USA
2. FAC MED STRASBOURG, CNRS, GENET MOLEC LAB, INSERM, U184, F-67085 STRASBOURG, FRANCE
Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON, ENGLAND N1 9XW
Subject Category: Multidisciplinary Sciences
IDS Number: JJ882
ISSN: 0028-0836
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