NDLI: GreA protein: a transcription elongation factor from Escherichia coli.

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GreA protein: a transcription elongation factor from Escherichia coli.

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GreA protein: a transcription elongation factor from Escherichia coli.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Nikiforov, V. Polyakov, A. Borukhov, S. Goldfarb, A.
Description	Author Affiliation: Borukhov S ( Department of Microbiology, Columbia University College of Physicians and Surgeons, New York, NY 10032.);
Abstract	A protein identified as the 158-amino acid product of the greA gene was isolated from Escherichia coli. When added to a halted ternary transcription complex, the GreA protein induced cleavage and removal of the 3' proximal dinucleotide from the nascent RNA. The new 3' terminus generated by the cleavage could be extended into longer transcripts. GreA-mediated cleavage of a transcript appears to permit a ternary complex to resume transcription from a state of indefinite elongation arrest induced by a specific DNA site. The GreA protein tended to interact with RNA polymerase during purification and recycled between RNA polymerase molecules in the course of the in vitro cleavage reaction. Similar biochemical activities have been reported in eukaryotic RNA polymerases, indicating that transcript cleavage and restart of elongation may be a general transcriptional mechanism.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	19
Volume Number	89
Language	English
Publisher	National Academy of Sciences
Publisher Date	1992-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Proteins Metabolism DNA-Directed RNA Polymerases Escherichia Coli Transcription Factors Isolation & Purification Chromatography, Gel Chromatography, Ion Exchange Genetics Genes, Bacterial Molecular Weight Oligoribonucleotides RNA, Bacterial Transcription, Genetic Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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