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Cited by 107Genomics and Chromatin DynamicsRNA Research and SplicingRNA and protein synthesis mechanisms

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The increment of SII-facilitated transcript cleavage varies dramatically between elongation competent and incompetent RNA polymerase II ternary complexes

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Izban, M.G., Luse, D.S.·1993·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(18)31468-6
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Abstract

Elongation factor SII is required to increase the efficiency of transcription by RNA polymerase II through intrinsic arrest sites. RNA polymerase II ternary complexes exhibit a ribonuclease activity in the presence of SII, truncating nascent transcripts in a 3'-->5' direction. We show here that transcript cleavage is an obligatory step in re-establishing the elongation competency of complexes that have become blocked in elongation at an intrinsic arrest site. SII-facilitated transcript cleavage by these arrested complexes released 7-14 nucleotide RNA fragments. In contrast, SII-facilitated transcript cleavage by elongation competent complexes, which are stalled because of the absence of a nucleoside triphosphate from the reaction mixture, occurred primarily in dinucleotide increments. We can partially recreate the arrested phenotype and the preference for the large cleavage increment by stalling ternary complexes such that the 3'-end of the transcript contains consecutive U residues, which mimics the sequence of the 3'-ends of transcripts in arrested complexes.

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Crossref · 10.1016/s0021-9258(18)31468-6

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Metadata

Authors
Izban, M. G., & Luse, D. S.
Affiliations
University of Cincinnati (US)
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1993-06
Volume
268
Issue
17
Pages
12874-12885
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(18)31468-6
OpenAlex
W1485158076
Cited by
107
References
34
Citations by year
2026: 1 · 2025: 1 · 2024: 3 · 2023: 1 · 2021: 1 · 2018: 3 · 2014: 1 · 2013: 1 · 2012: 2
FWCI
3.99
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5f32gm014111-02)
  • National Institute of General Medical Sciences (GM 14111, R01GM029487, GM 29487)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords
RNA polymerase II, transcript cleavage, transcription elongation, ternary complex, 3' end processing
MeSH terms
Animals, Base Sequence, Cattle, Humans, Molecular Sequence Data, Oligodeoxyribonucleotides, Plasmids, Protein Binding, RNA Polymerase II, RNA, Messenger, Transcription Factors, Transcription, Genetic, Dinucleoside Phosphates, Transcription Factors, General, Transcriptional Elongation Factors

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