The DOI matches its Crossref record; 79 of the 79 references it cites were found in a registry or an index.
DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs
Open accessAbstract
We report the identification of a transcription elongation factor from HeLa cell nuclear extracts that causes pausing of RNA polymerase II (Pol II) in conjunction with the transcription inhibitor 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole (DRB). This factor, termed DRB sensitivity-inducing factor (DSIF), is also required for transcription inhibition by H8. DSIF has been purified and is composed of 160-kD (p160) and 14-kD (p14) subunits. Isolation of a cDNA encoding DSIF p160 shows it to be a homolog of the Saccharomyces cerevisiae transcription factor Spt5. Recombinant Supt4h protein, the human homolog of yeast Spt4, is functionally equivalent to DSIF p14, indicating that DSIF is composed of the human homologs of Spt4 and Spt5. In addition to its negative role in elongation, DSIF is able to stimulate the rate of elongation by RNA Pol II in a reaction containing limiting concentrations of ribonucleoside triphosphates. A role for DSIF in transcription elongation is further supported by the fact that p160 has a region homologous to the bacterial elongation factor NusG. The combination of biochemical studies on DSIF and genetic analysis of Spt4 and Spt5 in yeast, also in this issue, indicates that DSIF associates with RNA Pol II and regulates its processivity in vitro and in vivo.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Phosphorylation of Ser5 of the Pol II CTD by transcription factor IIH (TFIIH) is required for transcription initiation, whereas phosphorylation of Ser2 of the Pol II CTD, of DSIF (DRB sensitivity inducing factor) and of NELF (negative elongation factor) by pTEFb (positive transcription elongation factor) is needed for transcription elongation141–143.”
From Molecular regulation of stem cell quiescence (2013) · cites this paper as [141]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Antibodies, a laboratory manual
(1989) · Biomedicine & Pharmacotherapy · doi:10.1016/0753-3322(89)90130-3 · Cited by 12,318
Dignam, J. D., Lebovitz, R. M., & Roeder, R. G. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.5.1475 · Cited by 11,262
Multiple sequence alignment with hierarchical clustering.
Corpet, F. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.22.10881 · Cited by 5,575
Frohman, M. A., Dush, M. K., & Martin, G. R. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.23.8998 · Cited by 4,554
Hidaka, H., Inagaki, M., Kawamoto, S., & Sasaki, Y. (1984) · Biochemistry · doi:10.1021/bi00316a032 · Cited by 2,688
The role of general initiation factors in transcription by RNA polymerase II
ROEDER, R. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)10050-5 · Cited by 1,009
Transcription elongation factor P-TEFb is required for HIV-1 Tat transactivation in vitroPreprint
Zhu, Y., Peery, T., Peng, J., Ramanathan, Y., Marshall, N. F., Marshall, T. K., Amendt, B. A., Mathews, M. B., & Price, D. H. (1997) · Genes & Development · doi:10.1101/gad.11.20.2622 · Cited by 700
Rougvie, A. E., & Lis, J. T. (1988) · Cell · doi:10.1016/s0092-8674(88)91087-2 · Cited by 680
Control of RNA Polymerase II Elongation Potential by a Novel Carboxyl-terminal Domain Kinase
Marshall, N. F., Peng, J., Xie, Z., & Price, D. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.43.27176 · Cited by 662
Yeast SNF/SWI transcriptional activators and the SPT/SIN chromatin connection
Winston, F., & Carlson, M. (1992) · Trends in Genetics · doi:10.1016/0168-9525(92)90300-s · Cited by 574
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Items 701–751 of 751
Chiang, C. (2010) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.2152956.1756055
Reduced polymerase pausing compensates for increased chromatin accessibility in the aging liverPreprint
Bozukova, M., Grbavac, D., Nikopoulou, C., & Tessarz, P. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.02.25.481984
Reines, D. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.732815397.793578919
Wood, W. (2015) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.725780196.793512076
Transcription | Transcription Termination
Sanders, T. J., Marshall, C. J., Wenck, B. R., Selan, J. N., & Santangelo, T. J. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819460-7.00129-8
Collin, A., González-Jiménez, A., González-Jiménez, M. D. C., Alfonso, M. J., & Calvo, O. (2022) · Cells · doi:10.3390/cells11203320
An essential signaling function of cytoplasmic NELFB is independent of RNA polymerase II pausing
Pan, H., Cheng, X., Rodríguez, P. F. G., Zhang, X., Chung, I., Jin, V. X., Li, W., Hu, Y., & Li, R. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105259
The Consequences of Contaminant miRNAs in Secreted Media Analysis
Thurnell, B. (2023) · Open Access Victoria University of Wellington | Te Herenga Waka (Figshare) · doi:10.26686/wgtn.24225304
Rtf1-dependent transcriptional pausing regulates cardiogenesisPreprint
Langenbacher, A. D., Lu, F., Tsang, L., Huang, Z. Y. S., Keer, B., Tian, Z., Eide, A., Pellegrini, M. A., Nakano, H., Nakano, A., et al. (2024) · eLife · doi:10.7554/elife.94524.1
Structural and biochemical studies on chromatin-protein complexes in transcription initiation
Garrido, J. A. (2024) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-10412
Ubiquitylation of RNA Polymerase II Controls Early Stages of the Transcription CyclePreprint
Cacioppo, R., Gillis, A., Shlamovitz, I., Zeller, A., Castiblanco, D., Crisp, A., Haworth, B., Arabiotorre, A., Abyaneh, P., Bao, Y., et al. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4826625
Morse, R. H. (2024) · Elsevier eBooks · doi:10.1016/b978-0-12-814809-9.00009-3
Mooney, R. A., Zhu, J., Saba, J., & Landick, R. C. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4882915
Liu, M., Li, Y., Yuan, X. H., Rong, S., & Du, J. (2024) · Biochemistry and Cell Biology · doi:10.1139/bcb-2024-0094
Kuś, K., Nielsen, S., Zenkin, N., & Vasiljeva, L. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.17.628955
SPT5 regulates Pol II pausing and elongation in different ways at early versus late embryonic stagesPreprint
Dulja, A., Mayer, M., Engel, N. L., Golov, A. K., Forneris, M., Kherdjemil, Y., Feng, S., Viales, R. R., & Furlong, E. E. M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.06.674612
Molecular Basis for Impacts of DSIF on the Dynamics of RNA Polymerase II Elongation Complex
Amith, W. D., Bogart, B. M., & Dutagaci, B. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c01961
Au, A., Southers, A., Kuś, K., Schoemaker, N., Balıkçı, E., Hewes, C., Fournier, M. L., Aydin, E., Hassanein, S. S., Kilchert, C., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.17.694969
Jadlowsky, J. K. (2009) · OhioLink ETD Center (Ohio Library and Information Network)
Shersher, E., Lahiry, M., Alvarez-Trotta, A., Diluvio, G., Robbins, D. J., Shiekhattar, R., & Capobianco, A. J. (2021) · Figshare · doi:10.6084/m9.figshare.16664495
Additional file 2 of The chromatin remodeler Ino80 mediates RNAPII pausing site determination
Cheon, Y., Han, S., Kim, T., Hwang, D., & Lee, D. (2021) · Figshare · doi:10.6084/m9.figshare.16829345
Shersher, E., Lahiry, M., Alvarez-Trotta, A., Diluvio, G., Robbins, D. J., Shiekhattar, R., & Capobianco, A. J. (2021) · Figshare · doi:10.6084/m9.figshare.16664489
Shersher, E., Lahiry, M., Alvarez-Trotta, A., Diluvio, G., Robbins, D. J., Shiekhattar, R., & Capobianco, A. J. (2021) · Figshare · doi:10.6084/m9.figshare.16664498
Chapman, S. (2013) · University Library - University of Saskatchewan (University of Saskatchewan)
Shersher, E., Lahiry, M., Alvarez-Trotta, A., Diluvio, G., Robbins, D. J., Shiekhattar, R., & Capobianco, A. J. (2021) · Figshare · doi:10.6084/m9.figshare.16664492
Additional file 1 of The chromatin remodeler Ino80 mediates RNAPII pausing site determination
Cheon, Y., Han, S., Kim, T., Hwang, D., & Lee, D. (2021) · Figshare · doi:10.6084/m9.figshare.16829342
Cycline G, contrôle de la transcription et stabilité du développement
Dardalhon-Cuménal, D. (2015) · theses.fr (ABES) · doi:10.70675/a91e9af4z581dz489ez9767za2969ab64eaf
Développement d’une nouvelle classe d'agents de sortie de latence du VIH-1
Tong, P. B. V. (2019) · theses.fr (ABES) · doi:10.70675/4fde9bf2zfe81z4f23z825dzd95ee9c825db
Real time imaging of transcription reveals new features of cellular and viral promoters
Kozulic-Pirher, A. (2018) · theses.fr (ABES) · doi:10.70675/0099e36bz620ez43d7z9b47z2789ed360d73
Contrôle de l'expression génique par la RNP 7SK
Studniarek, C. (2019) · theses.fr (ABES) · doi:10.70675/4bab1779z812bz45d6zbcd4z9eea765b52e7
An RNA Signature Links Oxidative Stress To Cellular Senescence
Mullani, N. (2019) · theses.fr (ABES) · doi:10.70675/1babf95cz77a0z4561za6cdz6bf733f9f455
Development of a new mutation monitoring system in the yeast Saccharomyces cerevisiae
Sipos, E. H. (2021) · theses.fr (ABES) · doi:10.70675/863bfb65z9db2z4e87z8304zdcb028419729
FragLite mapping to identify the BRD4 recruitment site of P-TEFbPreprint
Hope, I., Heath, R., Baslé, A., Martin, M. P., Waring, M. J., Endicott, J., Noble, M. E. M., & Tatum, N. J. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.09.717428 · Cited by 1
Yin, L., Zhang, Z., Wang, Z., Yang, X., Shi, C., Wang, Y., Guo, Y., & Zhang, J. (2026) · Physical review. E · doi:10.1103/j778-39sg
G0 or no-G0: phosphatase control of quiescence and cell cycle entry
Robinson, E. A., & Barr, A. R. (2026) · Biochemical Society Transactions · doi:10.1042/bst20250091 · Cited by 1
Francette, A. M., Grover, A., Clark, N., & Arndt, K. M. (2026) · PLoS Biology · doi:10.1371/journal.pbio.3003855
Kim, H., Grassmann, S. A., Wong, W., Adams, N. M., Kanno, Y., O’Shea, J. J., Leslie, C. S., Rogatsky, I., & Sun, J. C.-Y. (2026) · The Journal of Experimental Medicine · doi:10.1084/jem.20250995
Origin and Evolution of Transcription Elongation Complexes
Osina, E. V., Korovina, A. N., Gerasimova, N. S., Sokolova, O. S., & Stanishneva-Konovalova, T. B. (2026) · BIOPHYSICS · doi:10.1134/s0006350926700041
Transcription initiation drives dosage compensation establishment and maintenance in male Drosophila
Oellers, R., Alexiadis, A., Sun, Y., Navandar, M., Kulkarni, T., Holz, H., Georgiev, P., Rabbani, L., Shvedunova, M., Erdogdu, N. U., et al. (2026) · Science Advances · doi:10.1126/sciadv.aec3865
The Mediator complex: co-transcriptional regulation and beyond
Yang, Y., Zheng, Y., Zhou, Q., & Wang, G. (2026) · RNA Biology · doi:10.1080/15476286.2026.2707734
RNA polymerase II removal: transcription quality control and gene regulation
Haworth, B., Abyaneh, P., & Vidaković, A. T. (2026) · Transcription · doi:10.1080/21541264.2026.2698182
Dulja, A., Mayer, M., Engel, N. L., Golov, A. K., Bender, K., Forneris, M., Kherdjemil, Y., Feng, S., Viales, R. R., & Furlong, E. E. M. (2026) · Developmental Cell · doi:10.1016/j.devcel.2026.08.008
Fong, N., Huynh, N., Erickson, B., Sheridan, R. M., Ramachandran, S., van der Schaar, M., & Bentley, D. L. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.18.752771
Zhang, G. (2026) · Gene · doi:10.1016/j.gene.2026.150422 · Cited by 1
Esc2 and Rad57 contribute to RNA polymerase II distribution at highly transcribed genes
Masumoto, H., Muto, H., Kurosaki, Y., & Niki, H. (2026) · Life Science Alliance · doi:10.26508/lsa.202603673
Synergistic transcriptional regulation of collagenase gene expression in chondrocytes
Macdonald, C. D. (2013)
Metadata
- Authors
- Wada, T., Takagi, T., Yamaguchi, Y., Ferdous, A., Imai, T., Hirose, S., Sugimoto, S., Yano, K., Hartzog, G. A., Winston, F., Buratowski, S., & Handa, H.
- Affiliations
- National Institute of Genetics (JP)
- ORCID
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 1998-02-01
- Volume
- 12
- Issue
- 3
- Pages
- 343-356
- ISSN
- 0890-9369 (ISSN-L)
- PMC
- PMC316480
- OpenAlex
- W2148917483
- Cited by
- 750
- References
- 77
- Citations by year
- 2026: 23 · 2025: 18 · 2024: 33 · 2023: 20 · 2022: 24 · 2021: 38 · 2020: 32 · 2019: 24 · 2018: 24 · 2017: 21 · 2016: 28 · 2015: 24 · 2014: 23 · 2013: 31 · 2012: 28
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Figshare (submittedVersion, cc-by)
- Tokyo Tech Research Repository (Tokyo Institute of Technology) (submittedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM032967, R37GM032967, GM 32967)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- DSIF, transcription elongation, RNA polymerase II, processivity, Spt4, Spt5, transcriptional pausing, HeLa cells, Saccharomyces cerevisiae, cDNA cloning
- MeSH terms
- Amino Acid Sequence, Chromosomal Proteins, Non-Histone, Dichlororibofuranosylbenzimidazole, Fungal Proteins, HeLa Cells, Humans, Molecular Sequence Data, Nuclear Proteins, RNA Polymerase II, Saccharomyces cerevisiae, Sensitivity and Specificity, Transcription Factors, Transcription, Genetic, Transcriptional Activation, Sequence Homology, Amino Acid, Nucleic Acid Synthesis Inhibitors, Saccharomyces cerevisiae Proteins, Transcriptional Elongation Factors
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
