Intrinsic transcript cleavage activity of RNA polymerase.
basic_science · Level V
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- Record sourced from PubMed, PMID 7538676.
- Also identified by PMC identifier 41991.
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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.
Medical subject headings
- Bacterial Proteins
- DNA-Directed RNA Polymerases
- Escherichia coli
- Escherichia coli Proteins
- Peptide Elongation Factors
- RNA, Bacterial
- Transcription Factors
- Transcription, Genetic