ArticleThe Journal of biological chemistry1998
Recognition of a human arrest site is conserved between RNA polymerase II and prokaryotic RNA polymerases.
Article in The Journal of biological chemistry, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Analysis ofInfection and drug resistance · 2020Article
- Prediction ofSaudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2017Article
- Computational prediction of Mycoplasma hominis proteins targeting in nucleus of host cell and their implication in prostate cancer etiology.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Article
- Systems Biology Approaches for the Prediction of Possible Role of Chlamydia pneumoniae Proteins in the Etiology of Lung Cancer.PloS one · 2016Article
- Fluctuations, pauses, and backtracking in DNA transcription.Biophysical journal · 2008Article
- Transcription through chromatin by RNA polymerase II: histone displacement and exchange.Mutation research · 2007Review
- mRNA capping enzyme activity is coupled to an early transcription elongation.Molecular and cellular biology · 2004Article
- In vitro activity of the baculovirus late expression factor LEF-5.Journal of virology · 2002Article
- TFIIS enhances transcriptional elongation through an artificial arrest site in vivo.Molecular and cellular biology · 2001Article
- Analysis of gene induction and arrest site transcription in yeast with mutations in the transcription elongation machinery.The Journal of biological chemistry · 2001Article
- RNA polymerases from Bacillus subtilis and Escherichia coli differ in recognition of regulatory signals in vitro.Journal of bacteriology · 2000Article
- Pausing by bacterial RNA polymerase is mediated by mechanistically distinct classes of signals.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
DNA sequences that arrest transcription by either eukaryotic RNA polymerase II or Escherichia coli RNA polymerase have been identified previously. Elongation factors SII and GreB are RNA polymerase-binding proteins that enable readthrough of arrest sites by these enzymes, respectively. This functional similarity has led to general models of elongation applicable to both eukaryotic and prokaryotic enzymes. Here we have transcribed with phage and bacterial RNA polymerases, a human DNA sequence previously defined as an arrest site for RNA polymerase II. The phage and bacterial enzymes both respond efficiently to the arrest signal in vitro at limiting levels of nucleoside triphosphates. The E. coli polymerase remains in a template-engaged complex for many hours, can be isolated, and is potentially active. The enzyme displays a relatively slow first-order loss of elongation competence as it dwells at the arrest site. Bacterial RNA polymerase arrested at the human site is reactivated by GreB in the same way that RNA polymerase II arrested at this site is stimulated by SII. Very efficient readthrough can be achieved by phage, bacterial, and eukaryotic RNA polymerases in the absence of elongation factors if 5-Br-UTP is substituted for UTP. These findings provide additional and direct evidence for functional similarity between prokaryotic and eukaryotic transcription elongation and readthrough mechanisms.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.