메뉴 건너뛰기




Volumn 25, Issue 9, 2005, Pages 3583-3595

Human RNA polymerase II elongation in slow motion: Role of the TFIIF RAP74 α1 helix in nucleoside triphosphate-driven translocation

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; NUCLEOSIDE; PHOSPHATE; RNA POLYMERASE II; TRANSCRIPTION FACTOR IIH;

EID: 17644384843     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.25.9.3583-3595.2005     Document Type: Article
Times cited : (23)

References (45)
  • 3
    • 0026065031 scopus 로고
    • Role of the mammalian transcription factors IIF, IIS, and IIX during elongation by RNA polymerase II
    • Bengal, E., O. Flores, A. Krauskopf, D. Reinberg, and Y. Aloni. 1991. Role of the mammalian transcription factors IIF, IIS, and IIX during elongation by RNA polymerase II. Mol. Cell. Biol. 11:1195-1206.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1195-1206
    • Bengal, E.1    Flores, O.2    Krauskopf, A.3    Reinberg, D.4    Aloni, Y.5
  • 4
    • 0024600231 scopus 로고
    • A multisubunit transcription factor essential for accurate initiation by RNA polymerase II
    • Conaway, J. W., and R. C. Conaway. 1989. A multisubunit transcription factor essential for accurate initiation by RNA polymerase II. J. Biol. Chem. 264:2357-2362.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2357-2362
    • Conaway, J.W.1    Conaway, R.C.2
  • 5
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution
    • Cramer, P., D. A. Bushnell, and R. D. Kornberg. 2001. Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution. Science 292:1863-1876.
    • (2001) Science , vol.292 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 6
    • 0037125947 scopus 로고    scopus 로고
    • Use of 2-aminopurine and tryptophan fluorescence as probes in kinetic analyses of DNA polymerase Beta
    • Dunlap, C. A., and M. D. Tsai. 2002. Use of 2-aminopurine and tryptophan fluorescence as probes in kinetic analyses of DNA polymerase Beta. Biochemistry 41:11226-11235.
    • (2002) Biochemistry , vol.41 , pp. 11226-11235
    • Dunlap, C.A.1    Tsai, M.D.2
  • 7
    • 0025721103 scopus 로고
    • The small subunit of transcription factor IIF recruits RNA polymerase II into the preinitiation complex
    • Flores, O., H. Lu, M. Killeen, J. Greenblatt, Z. F. Burton, and D. Reinberg. 1991. The small subunit of transcription factor IIF recruits RNA polymerase II into the preinitiation complex. Proc. Natl. Acad. Sci. USA 88:9999-10003.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9999-10003
    • Flores, O.1    Lu, H.2    Killeen, M.3    Greenblatt, J.4    Burton, Z.F.5    Reinberg, D.6
  • 8
    • 0023814881 scopus 로고
    • Factors involved in specific transcription by mammalian RNA polymerase II. RNA polymerase II-associating protein 30 is an essential component of transcription factor IIF
    • Flores, O., E. Maldonado, Z. Burton, J. Greenblatt, and D. Reinberg. 1988. Factors involved in specific transcription by mammalian RNA polymerase II. RNA polymerase II-associating protein 30 is an essential component of transcription factor IIF. J. Biol. Chem. 263:10812-10816.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10812-10816
    • Flores, O.1    Maldonado, E.2    Burton, Z.3    Greenblatt, J.4    Reinberg, D.5
  • 9
    • 0035958552 scopus 로고    scopus 로고
    • Allosteric binding of nucleotide triphosphates to RNA polymerase regulates transcription elongation
    • Foster, J. E., S. F. Holmes, and D. A. Erie. 2001. Allosteric binding of nucleotide triphosphates to RNA polymerase regulates transcription elongation. Cell 106:243-252.
    • (2001) Cell , vol.106 , pp. 243-252
    • Foster, J.E.1    Holmes, S.F.2    Erie, D.A.3
  • 10
    • 0037033094 scopus 로고    scopus 로고
    • A key role for the alpha 1 helix of human RAP74 in the initiation and elongation of RNA chains
    • Funk, J. D., Y. A. Nedialkov, D. Xu, and Z. F. Burton. 2002. A key role for the alpha 1 helix of human RAP74 in the initiation and elongation of RNA chains. J. Biol. Chem. 277:46998-47003.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46998-47003
    • Funk, J.D.1    Nedialkov, Y.A.2    Xu, D.3    Burton, Z.F.4
  • 11
    • 0034613012 scopus 로고    scopus 로고
    • Novel dimerization fold of RAP30/RAP74 in human TFHF at 1.7 a resolution
    • Gaiser, F., S. Tan, and T. J. Richmond. 2000. Novel dimerization fold of RAP30/RAP74 in human TFHF at 1.7 A resolution. J. Mol. Biol. 302:1119-1127.
    • (2000) J. Mol. Biol. , vol.302 , pp. 1119-1127
    • Gaiser, F.1    Tan, S.2    Richmond, T.J.3
  • 12
    • 0037073076 scopus 로고    scopus 로고
    • Elongation by RNA polymerase II: Structure-function relationship
    • Gnatt, A. 2002. Elongation by RNA polymerase II: structure-function relationship. Biochim. Biophys. Acta 1577:175-190.
    • (2002) Biochim. Biophys. Acta , vol.1577 , pp. 175-190
    • Gnatt, A.1
  • 13
    • 0035827332 scopus 로고    scopus 로고
    • Structural basis of transcription: An RNA polymerase II elongation complex at 3.3 a resolution
    • Gnatt, A. L., P. Cramer, J. Fu, D. A. Bushnell, and R. D. Kornberg. 2001. Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution. Science 292:1876-1882.
    • (2001) Science , vol.292 , pp. 1876-1882
    • Gnatt, A.L.1    Cramer, P.2    Fu, J.3    Bushnell, D.A.4    Kornberg, R.D.5
  • 14
    • 3042595545 scopus 로고    scopus 로고
    • Alpha-amanitin blocks translocation by human RNA polymerase H
    • Gong, X. Q., Y. A. Nedialkov, and Z. F. Burton. 2004. Alpha-amanitin blocks translocation by human RNA polymerase H. J. Biol. Chem. 279:27422-27427.
    • (2004) J. Biol. Chem. , vol.279 , pp. 27422-27427
    • Gong, X.Q.1    Nedialkov, Y.A.2    Burton, Z.F.3
  • 15
    • 0029559444 scopus 로고
    • Variation in the size of nascent RNA cleavage products as a function of transcript length and elongation competence
    • Gu, W., and D. Reines. 1995. Variation in the size of nascent RNA cleavage products as a function of transcript length and elongation competence. J. Biol. Chem. 270:30441-30447.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30441-30447
    • Gu, W.1    Reines, D.2
  • 16
    • 0027178662 scopus 로고
    • Mechanism of DmS-II-mediated pause suppression by Drosophila RNA polymerase II
    • Guo, H., and D. H. Price. 1993. Mechanism of DmS-II-mediated pause suppression by Drosophila RNA polymerase II. J. Biol. Chem. 268:18762-18770.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18762-18770
    • Guo, H.1    Price, D.H.2
  • 17
    • 0041315524 scopus 로고    scopus 로고
    • Downstream DNA sequence effects on transcription elongation. Allosteric binding of nucleotide triphosphates facilitates translocation via a ratchet motion
    • Holmes, S. F., and D. A. Erie. 2003. Downstream DNA sequence effects on transcription elongation. Allosteric binding of nucleotide triphosphates facilitates translocation via a ratchet motion. J. Biol. Chem. 278:35597-35608.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35597-35608
    • Holmes, S.F.1    Erie, D.A.2
  • 18
    • 0026629273 scopus 로고
    • Factor-stimulated RNA polymerase II transcribes at physiological elongation rates on naked DNA but very poorly on chromatin templates
    • Izban, M. G., and D. S. Luse. 1992. Factor-stimulated RNA polymerase II transcribes at physiological elongation rates on naked DNA but very poorly on chromatin templates. J. Biol. Chem. 267:13647-13655.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13647-13655
    • Izban, M.G.1    Luse, D.S.2
  • 19
    • 0027163013 scopus 로고
    • The increment of SII-facilitated transcript cleavage varies dramatically between elongation competent and incompetent RNA polymerase II ternary complexes
    • Izban, M. G., and D. S. Luse. 1993. The increment of SII-facilitated transcript cleavage varies dramatically between elongation competent and incompetent RNA polymerase II ternary complexes. J. Biol. Chem. 268:12874-12885.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12874-12885
    • Izban, M.G.1    Luse, D.S.2
  • 20
    • 0026648570 scopus 로고
    • The RNA polymerase II ternary complex cleaves the nascent transcript in a 3′ → 5′ direction in the presence of elongation factor SII
    • Izban, M. G., and D. S. Luse. 1992. The RNA polymerase II ternary complex cleaves the nascent transcript in a 3′ → 5′ direction in the presence of elongation factor SII. Genes Dev. 6:1342-1356.
    • (1992) Genes Dev. , vol.6 , pp. 1342-1356
    • Izban, M.G.1    Luse, D.S.2
  • 21
    • 0028916224 scopus 로고
    • Rapid quench kinetic analysis of polymerases, adenosine triphosphatases, and enzyme intermediates
    • Johnson, K. A. 1995. Rapid quench kinetic analysis of polymerases, adenosine triphosphatases, and enzyme intermediates. Methods Enzymol. 249:38-61.
    • (1995) Methods Enzymol. , vol.249 , pp. 38-61
    • Johnson, K.A.1
  • 22
    • 0642315208 scopus 로고
    • Transient-state kinetic analysis of enzyme reaction pathways
    • Johnson, K. A. 1992. Transient-state kinetic analysis of enzyme reaction pathways. Enzymes 20:1-61.
    • (1992) Enzymes , vol.20 , pp. 1-61
    • Johnson, K.A.1
  • 23
    • 0043244876 scopus 로고    scopus 로고
    • Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage
    • Kettenberger, H., K. J. Armacbe, and P. Cramer. 2003. Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage. Cell 114:347-357.
    • (2003) Cell , vol.114 , pp. 347-357
    • Kettenberger, H.1    Armacbe, K.J.2    Cramer, P.3
  • 24
    • 10944232674 scopus 로고    scopus 로고
    • Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS
    • Kettenberger, H., K. J. Armache, and P. Cramer. 2004. Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS. Mol. Cell 16:955-965.
    • (2004) Mol. Cell , vol.16 , pp. 955-965
    • Kettenberger, H.1    Armache, K.J.2    Cramer, P.3
  • 25
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
    • Kuzmic, P. 1996. Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase. Anal. Biochem. 237:260-273.
    • (1996) Anal. Biochem. , vol.237 , pp. 260-273
    • Kuzmic, P.1
  • 26
    • 0033513098 scopus 로고    scopus 로고
    • The RAP74 subunit of human transcription factor HF has similar roles in initiation and elongation
    • Lei, L., D. Ren, and Z. F. Burton. 1999. The RAP74 subunit of human transcription factor HF has similar roles in initiation and elongation. Mol. Cell. Biol. 19:8372-8382.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8372-8382
    • Lei, L.1    Ren, D.2    Burton, Z.F.3
  • 29
    • 0345047725 scopus 로고    scopus 로고
    • Ubiquitous transcriptional pausing is independent of RNA polymerase backtracking
    • Neuman, K. C., E. A. Abbondanzieri, R. Landick, J. Gelles, and S. M. Block. 2003. Ubiquitous transcriptional pausing is independent of RNA polymerase backtracking. Cell 115:437-447.
    • (2003) Cell , vol.115 , pp. 437-447
    • Neuman, K.C.1    Abbondanzieri, E.A.2    Landick, R.3    Gelles, J.4    Block, S.M.5
  • 30
    • 0035838977 scopus 로고    scopus 로고
    • Roles of RNA:DNA hybrid stability, RNA structure, and active site conformation in pausing by human RNA polymerase II
    • Palangat, M., and R. Landick. 2001. Roles of RNA:DNA hybrid stability, RNA structure, and active site conformation in pausing by human RNA polymerase II. J. Mol. Biol. 311:265-282.
    • (2001) J. Mol. Biol. , vol.311 , pp. 265-282
    • Palangat, M.1    Landick, R.2
  • 31
    • 0032695884 scopus 로고    scopus 로고
    • A region within the RAP74 subunit of human transcription factor IIF is critical for initiation but dispensable for complex assembly
    • Ren, D., L. Lel, and Z. F. Burton. 1999. A region within the RAP74 subunit of human transcription factor IIF is critical for initiation but dispensable for complex assembly. Mol. Cell. Biol. 19:7377-7387.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7377-7387
    • Ren, D.1    Lel, L.2    Burton, Z.F.3
  • 32
    • 0035834647 scopus 로고    scopus 로고
    • A highly purified RNA polymerase II elongation control system
    • Renner, D. B., Y. Yamaguchi, T. Wada, H. Handa, and D. H. Price. 2001. A highly purified RNA polymerase II elongation control system. J. Biol. Chem. 276:42601-12609.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42601-112609
    • Renner, D.B.1    Yamaguchi, Y.2    Wada, T.3    Handa, H.4    Price, D.H.5
  • 33
    • 0346258014 scopus 로고    scopus 로고
    • Backtracking by single RNA polymerase molecules observed at near-base-pair resolution
    • Shaevitz, J. W., E. A. Abbondanzieri, R. Landick, and S. M. Block. 2003. Backtracking by single RNA polymerase molecules observed at near-base-pair resolution. Nature 426:684-687.
    • (2003) Nature , vol.426 , pp. 684-687
    • Shaevitz, J.W.1    Abbondanzieri, E.A.2    Landick, R.3    Block, S.M.4
  • 34
    • 0023835505 scopus 로고
    • A high-efficiency HeLa cell nuclear transcription extract
    • Shapiro, D. J., P. A. Sharp, W. W. Wahli, and M. J. Keller. 1988. A high-efficiency HeLa cell nuclear transcription extract. DNA 7:47-55.
    • (1988) DNA , vol.7 , pp. 47-55
    • Shapiro, D.J.1    Sharp, P.A.2    Wahli, W.W.3    Keller, M.J.4
  • 35
    • 0022360597 scopus 로고
    • Isolation of three proteins that bind to mammalian RNA polymerase II
    • Sopta, M., R. W. Carthew, and J. Greenblatt. 1985. Isolation of three proteins that bind to mammalian RNA polymerase II. J. Biol. Chem. 260:10353-10360.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10353-10360
    • Sopta, M.1    Carthew, R.W.2    Greenblatt, J.3
  • 36
    • 0037543997 scopus 로고    scopus 로고
    • Unified two-metal mechanism of RNA synthesis and degradation by RNA polymerase
    • Sosunov, V., E. Sosunova, A. Mustaev, I. Bass, V. Nikiforov, and A. Goldfarb. 2003. Unified two-metal mechanism of RNA synthesis and degradation by RNA polymerase. EMBO J. 22:2234-2244.
    • (2003) EMBO J. , vol.22 , pp. 2234-2244
    • Sosunov, V.1    Sosunova, E.2    Mustaev, A.3    Bass, I.4    Nikiforov, V.5    Goldfarb, A.6
  • 37
    • 0027943675 scopus 로고
    • Roles for both the RAP30 and RAP74 subunits of transcription factor HF in transcription initiation and elongation by RNA polymerase II
    • Tan, S., T. Aso, R. C. Conaway, and J. W. Conaway. 1994. Roles for both the RAP30 and RAP74 subunits of transcription factor HF in transcription initiation and elongation by RNA polymerase II. J. Biol. Chem. 269:25684-25691.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25684-25691
    • Tan, S.1    Aso, T.2    Conaway, R.C.3    Conaway, J.W.4
  • 38
    • 0029034913 scopus 로고
    • Dissection of transcription factor TFIIF functional domains required for initiation and elongation
    • Tan, S., R. C. Conaway, and J. W. Conaway. 1995. Dissection of transcription factor TFIIF functional domains required for initiation and elongation. Proc. Natl. Acad. Sci. USA 92:6042-6046.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6042-6046
    • Tan, S.1    Conaway, R.C.2    Conaway, J.W.3
  • 41
    • 0028518550 scopus 로고
    • Importance of codon preference for production of human RAP74 and reconstitution of the RAP30/74 complex
    • Wang, B. Q., L. Lei, and Z. F. Burton. 1994. Importance of codon preference for production of human RAP74 and reconstitution of the RAP30/74 complex. Protein Expression Purif. 5:476-485.
    • (1994) Protein Expression Purif. , vol.5 , pp. 476-485
    • Wang, B.Q.1    Lei, L.2    Burton, Z.F.3
  • 42
    • 8344234112 scopus 로고    scopus 로고
    • Structural basis of transcription; nucleotide selection by rotation in the RNA polymerase II active center
    • Westover, K. D., D. A. Bushnell, and R. D. Kornberg. 2004. Structural basis of transcription; nucleotide selection by rotation in the RNA polymerase II active center. Cell 119:481-189.
    • (2004) Cell , vol.119 , pp. 481-1189
    • Westover, K.D.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 43
    • 4444228491 scopus 로고    scopus 로고
    • Transcription factors IIF and IIS and nucleoside triphosphate substrates as dynamic probes of the human RNA polymerase II mechanism
    • Zhang, C., and Z. F. Burton. 2004. Transcription factors IIF and IIS and nucleoside triphosphate substrates as dynamic probes of the human RNA polymerase II mechanism. J. Mol. Biol. 342:1085-1099.
    • (2004) J. Mol. Biol. , vol.342 , pp. 1085-1099
    • Zhang, C.1    Burton, Z.F.2
  • 44
    • 0346749472 scopus 로고    scopus 로고
    • Combinatorial control of human RNA polymerase II (RNAP II) pausing and transcript cleavage by transcription factor IIF, hepatitis δ antigen, and stimulatory factor II
    • Zhang, C., H. Yan, and Z. F. Burton. 2003. Combinatorial control of human RNA polymerase II (RNAP II) pausing and transcript cleavage by transcription factor IIF, hepatitis δ antigen, and stimulatory factor II. J. Biol. Chem. 278:50101-50111.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50101-50111
    • Zhang, C.1    Yan, H.2    Burton, Z.F.3
  • 45
    • 0033578701 scopus 로고    scopus 로고
    • Crystal structure of Thermus aquations core RNA polymerase at 3.3 a resolution
    • Zhang, G., E. A. Campbell, L. Minakhin, C. Richter, K. Severinov, and S. A. Darst. 1999. Crystal structure of Thermus aquations core RNA polymerase at 3.3 A resolution. Cell 98:811-824.
    • (1999) Cell , vol.98 , pp. 811-824
    • Zhang, G.1    Campbell, E.A.2    Minakhin, L.3    Richter, C.4    Severinov, K.5    Darst, S.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.