NELF, a Multisubunit Complex Containing RD, Cooperates with DSIF to Repress RNA Polymerase II Elongation

Yamaguchi, Yuki; Takagi, Toshiyuki; Wada, Tadashi; Yano, Keiichi; Furuya, Akiko; Sugimoto, Seiji; Hasegawa, Jun; Handa, Hiroshi

doi:10.1016/s0092-8674(00)80713-8

Cited by 841Genomics and Chromatin DynamicsRNA Research and SplicingNuclear Structure and Function

NELF, a Multisubunit Complex Containing RD, Cooperates with DSIF to Repress RNA Polymerase II Elongation

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Yamaguchi, Yuki, Takagi, Toshiyuki, Wada, Tadashi, Yano, Keiichi, Furuya, Akiko, Sugimoto, Seiji, Hasegawa, Jun, Handa, Hiroshi·1999·Cell

DOI 10.1016/s0092-8674(00)80713-8

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Abstract

DRB is a classic inhibitor of transcription elongation by RNA polymerase II (pol II). Since DRB generally affects class II genes, factors involved in this process must play fundamental roles in pol II elongation. Recently, two elongation factors essential for DRB action were identified, namely DSIF and P-TEFb. Here we describe the identification and purification from HeLa nuclear extract of a third protein factor required for DRB-sensitive transcription. This factor, termed negative elongation factor (NELF), cooperates with DSIF and strongly represses pol II elongation. This repression is reversed by P-TEFb-dependent phosphorylation of the pol II C-terminal domain. NELF is composed of five polypeptides, the smallest of which is identical to RD, a putative RNA-binding protein of unknown function. This study reveals a molecular mechanism for DRB action and a regulatory network of positive and negative elongation factors.

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Phosphorylation of Ser2 of the Pol II CTD, DSIF, and NELF by pTEFb is needed for transcription elongation.
“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 [142]

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 · see citing works
Current protocols in molecular biology
Sargent, T. (1988) · Analytical Biochemistry · doi:10.1016/0003-2697(88)90147-9 · Cited by 7,281 · see citing works
Transcriptional regulation
Helntz, N. (1991) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(91)90161-n · Cited by 892 · see citing works
DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs
Wada, T., Takagi, T., Yamaguchi, Y., Ferdous, A., Imai, T., Hirose, S., Sugimoto, S., Yano, K., Hartzog, G. A., Winston, F., et al. (1998) · Genes & Development · doi:10.1101/gad.12.3.343 · Cited by 750 · see citing works
Self-citation
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 · see citing works
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 · see citing works
CONTROL OF RNA INITIATION AND ELONGATION AT THE HIV-1 PROMOTER
Jones, K. A., & Peterlin, B. M. (1994) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.63.070194.003441 · Cited by 618 · see citing works
Purification of P-TEFb, a Transcription Factor Required for the Transition into Productive Elongation
Marshall, N. F., & Price, D. H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.21.12335 · Cited by 564 · see citing works
5′-Capping enzymes are targeted to pre-mRNA by binding to the phosphorylated carboxy-terminal domain of RNA polymerase IIPreprint
McCracken, S. A., Fong, N., Rosonina, E., Yankulov, K., Brothers, G. M., Siderovski, D. P., Hessel, A., Foster, S., Program, A. E., Shuman, S., et al. (1997) · Genes & Development · doi:10.1101/gad.11.24.3306 · Cited by 548 · see citing works
Identification of multiple cyclin subunits of human P-TEFb.Preprint
Peng, J.-M., Zhu, Y., Milton, J. T., & Price, D. (1998) · Genes & Development · doi:10.1101/gad.12.5.755 · Cited by 531 · see citing works
Reversible Phosphorylation of the C-terminal Domain of RNA Polymerase II
Dahmus, M. E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.32.19009 · Cited by 501 · see citing works
Elongator, a Multisubunit Component of a Novel RNA Polymerase II Holoenzyme for Transcriptional Elongation
Otero, G., Fellows, J., Li, Y., de Bizemont, T., Dirac, A. M. G., Gustafsson, C. M., Erdjument‐Bromage, H., Tempst, P., & Svejstrup, J. Q. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80179-3 · Cited by 482 · see citing works
mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domainPreprint
Cho, E., Takagi, T., Moore, C. R., & Buratowski, S. (1997) · Genes & Development · doi:10.1101/gad.11.24.3319 · Cited by 478 · see citing works
Self-citation
Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiaePreprint
Hartzog, G. A., Wada, T., Handa, H., & Winston, F. (1998) · Genes & Development · doi:10.1101/gad.12.3.357 · Cited by 461 · see citing works
Self-citation
BASIC MECHANISMS OF TRANSCRIPT ELONGATION AND ITS REGULATION
Uptain, S. M., Kane, C. M., & Chamberlin, M. J. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.117 · Cited by 445 · see citing works
Factors involved in specific transcription by human RNA polymerase II: analysis by a rapid and quantitative in vitro assay.
Sawadogo, M., & Roeder, R. G. (1985) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.82.13.4394 · Cited by 421 · see citing works
Temporal Regulation of RNA Polymerase II by Srb10 and Kin28 Cyclin-Dependent Kinases
Hengartner, C. J., Myer, V. E., Liao, S.-M., Wilson, C. J., Koh, S. S., & Young, R. A. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80112-4 · Cited by 408 · see citing works
Evidence that P‐TEFb alleviates the negative effect of DSIF on RNA polymerase II‐dependent transcription in vitro
Wada, T., Takagi, T., Yamaguchi, Y., Watanabe, D., & Handa, H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7395 · Cited by 355 · see citing works
Self-citation
Elongin (SIII): A Multisubunit Regulator of Elongation by RNA Polymerase II
Aso, T., Lane, W. S., Conaway, J. W., & Conaway, R. C. (1995) · Science · doi:10.1126/science.7660129 · Cited by 327 · see citing works
The nonphosphorylated form of RNA polymerase II preferentially associates with the preinitiation complex.
Lu, H., Flores, O. A., Weinmann, R. S., & Reinberg, D. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.22.10004 · Cited by 325 · see citing works
Phosphorylation of RNA polymerase II C-terminal domain and transcriptional elongation
O’Brien, T., Hardin, S. E., Greenleaf, A. L., & Lis, J. T. (1994) · Nature · doi:10.1038/370075a0 · Cited by 324 · see citing works
A hyperphosphorylated form of the large subunit of RNA polymerase II is associated with splicing complexes and the nuclear matrix.
Mortillaro, M. J., Blencowe, B. J., Wei, X., Nakayasu, H., Du, L., Warren, S. L., Sharp, P. A., & Berezney, R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.16.8253 · Cited by 322 · see citing works
Control of formation of two distinct classes of RNA polymerase II elongation complexes.
Marshall, N. F., & Price, D. H. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.5.2078 · Cited by 298 · see citing works
HIV‐1 Tat protein promotes formation of more‐processive elongation complexes.
Marciniak, R. A., & Sharp, P. A. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb04997.x · Cited by 290 · see citing works
5,6-Dichloro-1-β-D-ribofuranosylbenzimidazole inhibits transcription elongation by RNA polymerase II in vitro
Chodosh, L. A., Fire, A. Z., Samuels, M. E., & Sharp, P. A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94169-4 · Cited by 234 · see citing works
NAT, a Human Complex Containing Srb Polypeptides that Functions as a Negative Regulator of Activated Transcription
Sun, X., Zhang, Y., Cho, H. K., Rickert, P., Lees, E. M., Lane, W. S., & Reinberg, D. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80131-8 · Cited by 232 · see citing works
Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II
Yue, Z., Maldonado, E., Pillutla, R. C., Cho, H. K., Reinberg, D., & Shatkin, A. J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.12898 · Cited by 226 · see citing works
The inhibition of DRB (5,6-dichloro-1-β-d-ribofuranosylbenzimidazole) of hnRNA and mRNA production in HeLa cells
Sehgal, P. B., Darnell, J. E., Jr., & Tamm, I. (1976) · Cell · doi:10.1016/0092-8674(76)90092-1 · Cited by 203 · see citing works
The C-terminal repeat domain of RNA polymerase II largest subunit is essential in vivo but is not required for accurate transcription initiation in vitro.
Zehring, W. A., Lee, J. M., Weeks, J. R., Jokerst, R. S., & Greenleaf, A. L. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.3698 · Cited by 192 · see citing works
Transcription factor IIE binds preferentially to RNA polymerase IIa and recruits TFIIH: a model for promoter clearance.Preprint
Maxon, M. E., Goodrich, J. A., & Tjian, R. (1994) · Genes & Development · doi:10.1101/gad.8.5.515 · Cited by 187 · see citing works
SPT5, an Essential Gene Important for Normal Transcription in Saccharomyces cerevisiae, Encodes an Acidic Nuclear Protein with a Carboxy-Terminal Repeat
Swanson, M. S., Malone, E. A., & Winston, F. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.6.3009 · Cited by 183 · see citing works
Phosphorylation of C-terminal domain of RNA polymerase II is not required in basal transcription
Serizawa, H., Conaway, J. W., & Conaway, R. C. (1993) · Nature · doi:10.1038/363371a0 · Cited by 182 · see citing works
A CTD function linking transcription to splicing
Corden, J. L., & Patturajan, M. (1997) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01125-0 · Cited by 157 · see citing works
FCP1, the RAP74-Interacting Subunit of a Human Protein Phosphatase That Dephosphorylates the Carboxyl-terminal Domain of RNA Polymerase IIO
Archambault, J., Pan, G., Dahmus, G. K., Cartier, M., Marshall, N. F., Zhang, S., Dahmus, M. E., & Greenblatt, J. F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.42.27593 · Cited by 149 · see citing works
An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in Saccharomyces cerevisiae
Archambault, J., Chambers, R., Kobor, M. S., Ho, Y., Cartier, M., Bolotin, D., Andrews, B., Kane, C. M., & Greenblatt, J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.26.14300 · Cited by 145 · see citing works
Structure and Function of the Human Transcription Elongation Factor DSIF
Yamaguchi, Y., Wada, T., Watanabe, D., Takagi, T., Hasegawa, J., & Handa, H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.12.8085 · Cited by 143 · see citing works
Self-citation
The RNA polymerase II general elongation factors
Reines, D., Conaway, J. W., & Conaway, R. C. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)10045-1 · Cited by 135 · see citing works
A role for TFIIH in controlling the activity of early RNA polymerase II elongation complexes
Dvir, A., Conaway, R. C., & Conaway, J. W. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.17.9006 · Cited by 131 · see citing works
A kinase-deficient transcription factor TFIIH is functional in basal and activated transcription.
Mäkelä, T. P., Parvin, J. D., Kim, J., Huber, L. J., Sharp, P. A., & Weinberg, R. A. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.11.5174 · Cited by 123 · see citing works
Inhibitors of transcription such as 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole and isoquinoline sulfonamide derivatives (H-8 and H-7) promote dephosphorylation of the carboxyl-terminal domain of RNA polymerase II largest subunit.
Dubois, M., Nguyen, V. T., Bellier, S., & Bensaude, O. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36837-0 · Cited by 122 · see citing works
The Activity of COOH-terminal Domain Phosphatase Is Regulated by a Docking Site on RNA Polymerase II and by the General Transcription Factors IIF and IIB
Chambers, R., Wang, B. Q., Burton, Z. F., & Dahmus, M. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.25.14962 · Cited by 122 · see citing works
The RNA polymerase II general elongation factors
Reines, D. (1996) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(96)10045-1 · Cited by 114 · see citing works
A Previously Undetected MHC Gene with an Unusual Periodic Structure
Lévi‐Strauss, M., Carroll, M. C., Steinmetz, M., et al. (1988) · Science · doi:10.1126/science.3353717 · Cited by 106 · see citing works
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 · see citing works
Interplay between positive and negative elongation factors: drawing a new view of DRB
Yamaguchi, Y., Wada, T., & Handa, H. (1998) · Genes to Cells · doi:10.1046/j.1365-2443.1998.00162.x · Cited by 81 · see citing works
Self-citation
Transcription factor E4TF1 contains two subunits with different functions.
Watanabe, H., Wada, T., & Handa, H. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb08181.x · Cited by 79 · see citing works
Self-citation
SPT5, an Essential Gene Important for Normal Transcription in Saccharomyces cerevisiae, Encodes an Acidic Nuclear Protein with a Carboxy-Terminal Repeat
(1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.8.4286-.1991 · Cited by 79 · see citing works
Promoter-proximal stalling results from the inability to recruit transcription factor IIH to the transcription complex and is a regulated event
Kumar, K. P., Akoulitchev, S., & Reinberg, D. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.17.9767 · Cited by 76 · see citing works
47 Analysis of SPT Genes: A Genetic Approach toward Analysis of TFIID, Histones, and Other Transcription Factors of YeastPreprint
Winston, F. (1992) · Cold Spring Harbor Monograph Archive · doi:10.1101/087969425.22b.1271 · Cited by 64 · see citing works
A Human RNA Polymerase II Transcription Termination Factor Is a SWI2/SNF2 Family Member
Liu, M., Zhi, X., & Price, D. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.40.25541 · Cited by 59 · see citing works
Purification of an RNA Polymerase II Transcript Release Factor from Drosophila
Zhi, X., & Price, D. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.19.11043 · Cited by 52 · see citing works
Purification of RNA polymerase IIO from calf thymus.
Kim, W. Y., & Dahmus, M. E. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37364-2 · Cited by 49 · see citing works
Regulation of the human general transcription initiation factor TFIIF by phosphorylation.
Kitajima, S., Chibazakura, T., Yonaha, M., et al. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43976-2 · Cited by 46 · see citing works
Affinity purification of transcription factor IIA from HeLa cell nuclear extracts.
Usuda, Y., Kubota, A., Berk, A. J., & Handa, H. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07767.x · Cited by 44 · see citing works
Self-citation
Structural Changes in the RNA Polymerase II Transcription Complex during Transition from Initiation to Elongation
Samkurashvili, I., & Luse, D. S. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.9.5343 · Cited by 43 · see citing works
Identification and Analysis of a Functional Human Homolog of the SPT4 Gene of Saccharomyces cerevisiae
Hartzog, G. A., Basrai, M. A., Ricupero‐Hovasse, S. L., Hieter, P., & Winston, F. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.6.2848 · Cited by 38 · see citing works
Immunoaffinity purification of RNA polymerase II and transcription factors using polyol-responsive monoclonal antibodies
Thompson, N. E., & Burgess, R. R. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)74041-7 · Cited by 30 · see citing works
Different biological activities of the hetero- and homodimers formed by the 47- and 43-kilodalton proteins of transcription factor ATF/E4TF3
Wada, T., Watanabe, H., Usuda, Y., & Handa, H. (1991) · Journal of Virology · doi:10.1128/jvi.65.2.557-564.1991 · Cited by 24 · see citing works
Self-citation
cDNA cloning and characterization of the protein encoded by RD, a gene located in the class III region of the human major histocompatibility complex
Cheng, J., Macon, K. J., & Volanakis, J. E. (1993) · Biochemical Journal · doi:10.1042/bj2940589 · Cited by 20 · see citing works

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Authors: Yamaguchi, Y., Takagi, T., Wada, T., Yano, K., Furuya, A., Sugimoto, S., Hasegawa, J., & Handa, H.
Affiliations: Tokyo Institute of Technology (JP)
Corresponding author: Handa, Hiroshi
ORCID: Yamaguchi, Yuki
Yano, Keiichi
Handa, Hiroshi
Venue: Cell
Publisher: Elsevier BV
Published: 1999-04
Volume: 97
Issue: 1
Pages: 41-51
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/s0092-8674(00)80713-8
OpenAlex: W2162082053
Cited by: 841
References: 59
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FWCI: 10.91
Type: journal article
Language: en
Open access: bronze
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Locations: Cell (publishedVersion)
PubMed (publishedVersion)
Tokyo Tech Research Repository (Tokyo Institute of Technology) (submittedVersion)
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 › Nuclear Structure and Function
Keywords: NELF, DRB, RNA polymerase II elongation, DSIF, P-TEFb, C-terminal domain phosphorylation, class II genes, multisubunit complexes, HeLa cell nuclear extracts
MeSH terms: Amino Acid Sequence, Cloning, Molecular, Dichlororibofuranosylbenzimidazole, HeLa Cells, Humans, Kinetics, Molecular Sequence Data, Nuclear Proteins, Repressor Proteins, RNA Polymerase II, Transcription Factors, Tumor Cells, Cultured, RNA-Binding Proteins, Protein Serine-Threonine Kinases, Dimerization, Transcriptional Elongation Factors, Positive Transcriptional Elongation Factor B

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NELF, a Multisubunit Complex Containing RD, Cooperates with DSIF to Repress RNA Polymerase II Elongation

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