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DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs

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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.·1998·Genes & Development

DOI 10.1101/gad.12.3.343PMC PMC316480

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Abstract

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.

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Antibodies, a laboratory manual
(1989) · Biomedicine & Pharmacotherapy · doi:10.1016/0753-3322(89)90130-3 · Cited by 12,318
Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
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
Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer.
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
Isoquinolinesulfonamides, novel and potent inhibitors of cyclic nucleotide-dependent protein kinase and protein kinase C
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
The RNA polymerase II molecule at the 5′ end of the uninduced hsp70 gene of D. melanogaster is transcriptionally engaged
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
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Garber, M. E., Mayall, T. P., Suess, E. M., Meisenhelder, J., Thompson, N. E., & Jones, K. A. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.18.6958-6969.2000 · Cited by 151
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Moteki, S. A., & Price, D. H. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00660-3 · Cited by 150
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Denis, C. L., & Chen, J. (2003) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(03)01007-9 · Cited by 150
The transcription cycle in eukaryotes: From productive initiation to RNA polymerase II recycling
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Keegan, B. R., Feldman, J. L., Lee, D. H., Koos, D. S., Ho, R. K., Stainier, D. Y. R., & Yelon, D. L. (2002) · Development · doi:10.1242/dev.129.7.1623 · Cited by 106
Negative Elongation Factor Is Required for the Maintenance of Proviral Latency but Does Not Induce Promoter-Proximal Pausing of RNA Polymerase II on the HIV Long Terminal Repeat
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A genome-wide survey of RS domain proteins.
Boucher, L., Ouzounis, C. A., Enright, A. J., & Blencowe, B. J. (2001) · Europe PMC (PubMed Central) · Cited by 105
Core Histones and HIRIP3, a Novel Histone-Binding Protein, Directly Interact with WD Repeat Protein HIRA
Lorain, S., Quivy, J., Monier-Gavelle, F., Scamps, C., Lécluse, Y., Almouzni, G., & Lipinski, M. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.9.5546 · Cited by 105
Factors regulating the transcriptional elongation activity of RNA polymerase II
Shilatifard, A. (1998) · The FASEB Journal · doi:10.1096/fasebj.12.14.1437 · Cited by 104
DSIF and NELF interact with Integrator to specify the correct post-transcriptional fate of snRNA genes
Yamamoto, J., Hagiwara, Y., Chiba, K., Isobe, T., Narita, T., Handa, H., & Yamaguchi, Y. (2014) · Nature Communications · doi:10.1038/ncomms5263 · Cited by 104
Self-citation
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David, B. B. (2000) · Frontiers in bioscience · doi:10.2741/bregman · Cited by 103
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Ghose, R., Liou, L., Herrmann, C. H., & Rice, A. P. (2001) · Journal of Virology · doi:10.1128/jvi.75.23.11336-11343.2001 · Cited by 100
Transcriptional Pausing Caused by NELF Plays a Dual Role in Regulating Immediate-Early Expression of the junB Gene
Aida, M., Chen, Y., Nakajima, K., Yamaguchi, Y., Wada, T., & Handa, H. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.02366-05 · Cited by 105
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Egloff, S. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03878-8 · Cited by 104
The RNA polymerase II transcription cycle: cycling through chromatin
Svejstrup, J. Q. (2003) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/j.bbaexp.2003.10.012 · Cited by 99
Formation of a Carboxy-Terminal Domain Phosphatase (Fcp1)/TFIIF/RNA Polymerase II (pol II) Complex in Schizosaccharomyces pombe Involves Direct Interaction between Fcp1 and the Rpb4 Subunit of pol II
Kimura, M., Suzuki, H., & Ishihama, A. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.5.1577-1588.2002 · Cited by 99
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Conaway, J. W., & Conaway, R. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.301 · Cited by 99
Promoter proximal pausing on genes in metazoans
Gilmour, D. S. (2008) · Chromosoma · doi:10.1007/s00412-008-0182-4 · Cited by 95
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Liu, C.-R., Chang, C., Chern, Y., Wang, T.-H., Hsieh, W.-C., Shen, W.-C., Chang, C.-Y., Chu, I.-C., Deng, N., Cohen, S. N., et al. (2012) · Cell · doi:10.1016/j.cell.2011.12.032 · Cited by 93
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Self-citation

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: Yamaguchi, Y.
Ferdous, A.
Imai, T.
Hirose, S.
Yano, K.
Hartzog, G. A.
Winston, F.
Buratowski, S.
Handa, H.
Venue: Genes & Development
Publisher: Cold Spring Harbor Laboratory
Published: 1998-02-01
Volume: 12
Issue: 3
Pages: 343-356
ISSN: 0890-9369 (ISSN-L)
DOI: 10.1101/gad.12.3.343
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

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DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs

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