Intrinsic transcript cleavage activity of RNA polymerase

Marianna Orlova, Janet Newlands, Asis Das, Alex Goldfarb, Sergei Borukhov

Research output: Contribution to journalArticlepeer-review

177 Scopus citations

Abstract

The GreA and GreB transcript cleavage factors of Escherichia coli suppress elongation arrest and may have a proofreading role in transcription. With the use of E. coli greA-greB- mutant, RNA polymerase is demonstrated to possess substantial intrinsic transcript cleavage activity. Mildly alkaline pH mimics the effect of the Gre proteins by inducing transcript cleavage in ternary complexes and antagonizing elongation arrest through a cleavage-and-restart reaction. Thus, transcript cleavage constitutes the second enzymological activity of RNA polymerase along with polymerization/pyrophosphorolysis of RNA, whereas the Gre proteins merely enhance this intrinsic property.

Original languageEnglish (US)
Pages (from-to)4596-4600
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume92
Issue number10
DOIs
StatePublished - May 9 1995

All Science Journal Classification (ASJC) codes

  • General

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