Cited by 92Genomics and Chromatin DynamicsRNA and protein synthesis mechanismsForce Microscopy Techniques and Applications

Transcription factors TFIIF and TFIIS promote transcript elongation by RNA polymerase II by synergistic and independent mechanisms

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Schweikhard, Volker, Meng, Cong, Murakami, Kenji, Kaplan, Craig D., Kornberg, Roger D., Block, Steven M.·2014·Proceedings of the National Academy of Sciences

Abstract

Significance: In higher organisms, DNA is bound to proteins and tightly packed within the nucleus, leaving only certain regions accessible for gene expression. As the enzyme RNA polymerase II (RNAPII) travels along the DNA template synthesizing RNA, it must contend with forces generated by various obstacles, and some of these forces are known to produce transient pausing and even transcriptional arrest. How do organisms deal with such problems? Using optical-trapping technology, we performed a single-molecule study of RNAPII interactions with transcription factors TFIIS and TFIIF, which are involved in modulating and regulating transcriptional elongation. By applying controlled loads to RNAPII and combinations of these factors, we learned about the mechanisms by which pausing and arrest are overcome.

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  • TFIIS reduces the duration of pausing and accelerates RNA Pol II transcription in vitro.

    “TFIIS thus reduces the duration of pausing and has been shown to accelerate RNA Pol II transcription in vitro (Ishibashi et al, 2014; Schweikhard et al, 2014).”

    From RNA polymerase II speed: a key player in controlling and adapting transcriptome composition (2021) · cites this paper as Schweikhard et al, 2014

    The Effects of TFIIS and TFIIF Probed by ITP Misincorporation section reports that TFIIS shortened misincorporation-induced pauses, particularly with TFIIF present. But the RNAPII Elongation and Pausing section says TFIIS had no strong effect on pause-free elongation velocity, and the paper does not establish a general reduction in pause duration; under hindering loads, TFIIS increased the density of longer pauses. (LLM, conf=0.88)

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Authors
Schweikhard, V., Meng, C., Murakami, K., Kaplan, C. D., Kornberg, R. D., & Block, S. M.
Affiliations
  • Stanford University (US)
  • Chemistry,
  • Structural Biology, and
  • Texas A&M University (US)
Venue
Proceedings of the National Academy of Sciences
Published
2014-04-14
Volume
111
Issue
18
Pages
6642-6647
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2091727198
Cited by
92
References
52
Citations by year
2026: 6 · 2025: 2 · 2024: 11 · 2023: 5 · 2022: 7 · 2021: 10 · 2020: 8 · 2019: 8 · 2018: 10 · 2017: 8 · 2016: 9 · 2015: 4 · 2014: 3
FWCI
3.28
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • OakTrust (Texas A&M University Libraries) (submittedVersion)
Funders
  • National Institute of General Medical Sciences (GM 36659, R37GM057035, GM97260, R01GM097260, GM57035, R01GM057035, R37GM036659, R01GM036659)
  • National Institute of Allergy and Infectious Diseases (R01AI021144, AI 21144)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Force Microscopy Techniques and Applications
Keywords
RNA polymerase II, transcription elongation, TFIIF, TFIIS, transcription elongation factor, RNA polymerase pausing, backtracking, mechanical loading, transcript cleavage
MeSH terms
Enzyme Activation, Enzyme Reactivators, Inosine Triphosphate, Kinetics, Models, Biological, Recombinant Proteins, RNA Polymerase II, Saccharomyces cerevisiae, Transcription Factors, TFII, Saccharomyces cerevisiae Proteins, Transcriptional Elongation Factors, Optical Tweezers, Transcription Elongation, Genetic

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