The increment of SII-facilitated transcript cleavage varies dramatically between elongation competent and incompetent RNA polymerase II ternary complexes
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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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RNA Pol II cleaves the nascent RNA 3′ end, releasing an RNA fragment of 2-14 bases long and producing a new 3′ end perfectly aligned with its active site.
“RNA Pol II cleaves the nascent RNA 3′ end, releasing an RNA fragment of 2–14 bases long (Izban & Luse, 1993) and producing a new 3′ end perfectly aligned with its active site.”
From RNA polymerase II speed: a key player in controlling and adapting transcriptome composition (2021) · cites this paper as Izban & Luse, 1993
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“Released cleavage products range from 2 to 14 nt and this may relate to the extent of backtracking (9,12).”
BackgroundFeatures of yeast RNA polymerase I with special consideration of the lobe binding subunits
Schwank, K., Schmid, C., Fremter, T., Engel, C., Milkereit, P., Griesenbeck, J., & Tschochner, H. (2023) · Biological Chemistry · doi:10.1515/hsz-2023-0184 · Cited by 7 · see citing works
“To overcome the backtracked state to restart transcription elongation, Pols have to realign the 3 ′ end of the RNA with the active site either by one dimensional di ff usion or by RNA cleavage (Depken et al. 2009; Galburt et al. 2007; Izban and Luse 1993; Lisica et al. 2016; Reines 1992).”
Template End-to-End Transposition by RNA Polymerase II
Izban, M. G., Parsons, M. A., & Sinden, R. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.41.27009 · Cited by 7 · see citing works
Self-citationFuller, K. B., Jacobs, R. Q., Schneider, D. A., et al. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168606 · Cited by 5 · see citing works
Oh, Y., Yoon, J., & Baek, K. (1995) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(95)00055-l · Cited by 4 · see citing works
Murayama, Y., Sekine, S., & Yokoyama, S. (2013) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309113000055 · Cited by 2 · see citing works
“In the latter case, RNAP hydrolyses the RNA at its catalytic site to remove the protruding 30-end residues, allowing it to resume RNA elongation from the newly formed 30 end (Izban & Luse, 1993; Reines, 1992).”
Background
- Authors
- Izban, M. G., & Luse, D. S.
- Affiliations
- University of Cincinnati (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-06
- Volume
- 268
- Issue
- 17
- Pages
- 12874-12885
- ISSN
- 0021-9258 (ISSN-L)
- 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
- hybrid
- doi.org
- 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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