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Proc Natl Acad Sci U S A. 1995 May 9;92(10):4596-600.

Intrinsic transcript cleavage activity of RNA polymerase.

Author information

1
Public Health Research Institute, New York, NY 10016, USA.

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.

PMID:
7538676
PMCID:
PMC41991
DOI:
10.1073/pnas.92.10.4596
[Indexed for MEDLINE]
Free PMC Article

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