The DOI matches its Crossref record; 0 of the 34 references it cites were found in a registry or an index.
The increment of SII-facilitated transcript cleavage varies dramatically between elongation competent and incompetent RNA polymerase II ternary complexes
Open accessAbstract
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 (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
Citations
Cites
FASEB J
Kerppola (1991)
UnresolvedOncogene
Spencer (1990)
UnresolvedJ. Biol. Chem
Dedrick (1987)
UnresolvedBiochemistry
Kerppola (1990)
UnresolvedJ. Mol. Biol
Reines (1987)
UnresolvedJ. Biol. Chem
Reines (1989)
UnresolvedMol. Cell. Biol
Bengal (1991)
UnresolvedJ. Biol. Chem
Izban (1992)
UnresolvedJ. Biol. Chem
Wiest (1992)
UnresolvedJ. Biol. Chem
Resnekov (1989)
Unresolved
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Items 101–107 of 107
Crucial role of a dicarboxylic motif in the catalytic center of yeast RNA polymerases
Ruprich‐Robert, G., Wéry, M., Despres, D., Boulard, Y., & Thuriaux, P. (2011) · Current Genetics · doi:10.1007/s00294-011-0350-6 · Cited by 2
“Despite this strong conservation, the yeast dst1D deletion only leads to a slight cold-sensitive defect (Reines et al. 1989; Izban and Luse 1993; Kettenberger et al. 2004; Ghavi-Helm et al. 2008; Svejstrup 2010).”
BackgroundDomain acquisition enabled functional expansion of the TFIIS transcription factor family
Matveyeva, K., de Diego, A. S., García-López, M. Á., Gutiérrez, J., Fischer, T., & van Wely, K. H. M. (2025) · Cell & Bioscience · doi:10.1186/s13578-025-01423-9 · Cited by 1
“The changes in Pol2 induced by TFIIS indeed identified such a specific condition; biochemical studies showed that TFIIS binds to stalled Pol2, and promotes a reverse movement of up to 17 nucleotides of the latter [7, 65].”
Nucleotide-Dependent Degradation of Nucleic Acids by DNA and RNA Polymerases
Sosunov, V. V., & Victorova, L. S. (2004) · Molecular Biology · doi:10.1023/b:mbil.0000043938.36981.7d · Cited by 1
Kettenberger, H. (2005) · Electronic Theses of LMU Munich (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.3907
Translesion DNA Polymerase eta functions in transcription elongation
Gali, V. K. (2018) · SZTE Repository of Dissertations (University of Szeged) · doi:10.14232/phd.9838
Merkl, P., Pilsl, M., Fremter, T., Längst, G., Milkereit, P., Griesenbeck, J., & Tschochner, H. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/433375
“As published for Pol I and II transcription (Izban and Luse, 1993) (Lisica et al., 2016) and described above, different backtracking depths of ternary elongation complexes can occur.”
BackgroundTFIIS enhancement of Pol II cleavage is under kinetic control
Requijo, R. M., Maluf, N. K., Schneider, D. A., & Lucius, A. L. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag874
“In contrast to Pols I and III, transcription factor IIS (TFIIS) is a trans-acting factor that must be recruited to Pol II to confer endonuclease activity [ 7 , 8 , 34 , 35 ].”
Metadata
- 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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