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Volumn 2, Issue 5, 2003, Pages 1046-1052

Role of second-largest RNA polymerase I subunit Zn-binding domain in enzyme assembly

Author keywords

[No Author keywords available]

Indexed keywords

DNA DIRECTED RNA POLYMERASE; GALACTOSE; GLUCOSE; PROTEIN SUBUNIT; ZINC;

EID: 0142247060     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.2.5.1046-1052.2003     Document Type: Article
Times cited : (6)

References (37)
  • 1
    • 0022132080 scopus 로고
    • Extensive homology among the largest subunits of eukaryotic and prokaryotic RNA polymerases
    • Allison, L. A., M. Moyle, M. Shales, and C. J. Ingles. 1985. Extensive homology among the largest subunits of eukaryotic and prokaryotic RNA polymerases. Cell 42:599-610.
    • (1985) Cell , vol.42 , pp. 599-610
    • Allison, L.A.1    Moyle, M.2    Shales, M.3    Ingles, C.J.4
  • 2
    • 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
  • 4
    • 0034607658 scopus 로고    scopus 로고
    • Zinc stoichiometry of yeast RNA polymerase II and characterization of mutations in the zinc-binding domain of the largest subunit
    • Donaldson, I. M., and J. D. Friesen. 2000. Zinc stoichiometry of yeast RNA polymerase II and characterization of mutations in the zinc-binding domain of the largest subunit. J. Biol. Chem. 275:13780-13788.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13780-13788
    • Donaldson, I.M.1    Friesen, J.D.2
  • 6
    • 0033605419 scopus 로고    scopus 로고
    • Mutants in ABC10β, a conserved subunit shared by all three yeast RNA polymerases, specifically affect RNA polymerase I assembly
    • Gadal, O., G. V. Shpakovski, and P. Thuriaux. 1999. Mutants in ABC10β, a conserved subunit shared by all three yeast RNA polymerases, specifically affect RNA polymerase I assembly. J. Biol. Chem. 274:8421-8427.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8421-8427
    • Gadal, O.1    Shpakovski, G.V.2    Thuriaux, P.3
  • 7
    • 0037107455 scopus 로고    scopus 로고
    • Hmo1, an HMG-box protein, belongs to the yeast ribosomal DNA transcription system
    • Gadal, O., S. Labarre, C. Boschiero, and P. Thuriaux. 2002. Hmo1, an HMG-box protein, belongs to the yeast ribosomal DNA transcription system. EMBO J. 21:5498-5507.
    • (2002) EMBO J. , vol.21 , pp. 5498-5507
    • Gadal, O.1    Labarre, S.2    Boschiero, C.3    Thuriaux, P.4
  • 8
    • 0031001382 scopus 로고    scopus 로고
    • A34.5, a nonessential component of yeast RNA polymerase I, cooperates with subunit A14 and DNA topoisomerase I to produce a functional rRNA synthesis machine
    • Gadal, O., S. Mariotte-Labarre, S. Chedin, E. Quemeneur, C. Carles, A. Sentenac, and P. Thuriaux. 1997. A34.5, a nonessential component of yeast RNA polymerase I, cooperates with subunit A14 and DNA topoisomerase I to produce a functional rRNA synthesis machine. Mol. Cell. Biol. 17:1787-1795.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1787-1795
    • Gadal, O.1    Mariotte-Labarre, S.2    Chedin, S.3    Quemeneur, E.4    Carles, C.5    Sentenac, A.6    Thuriaux, P.7
  • 9
    • 0035827332 scopus 로고    scopus 로고
    • Structural basis of transcription: An RNA polymerase II elongation complex at 3.3 Å 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 Å 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
  • 10
    • 0032035316 scopus 로고    scopus 로고
    • Subunits of yeast RNA polymerases: Structure and function
    • Ishihama, A., M. Kimura, and H. Mitsuzawa. 1998. Subunits of yeast RNA polymerases: structure and function. Curr. Opin. Microbiol. 1:190-196.
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 190-196
    • Ishihama, A.1    Kimura, M.2    Mitsuzawa, H.3
  • 11
    • 0032509225 scopus 로고    scopus 로고
    • Reconstitution of yeast RNA polymerase I transcription in vitro from purified components. TATA-binding protein is not required for basal transcription
    • Keener, J., C. A. Josaitis, J. A. Dodd, and M. Nomura. 1998. Reconstitution of yeast RNA polymerase I transcription in vitro from purified components. TATA-binding protein is not required for basal transcription. J. Biol. Chem. 273:33795-33802.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33795-33802
    • Keener, J.1    Josaitis, C.A.2    Dodd, J.A.3    Nomura, M.4
  • 12
    • 0029609246 scopus 로고
    • Functional map of the alpha subunit of Escherichia coli RNA polymerase: Amino acid substitution within the amino-terminal assembly domain
    • Kimura, M., and A. Ishihama. 1995. Functional map of the alpha subunit of Escherichia coli RNA polymerase: amino acid substitution within the amino-terminal assembly domain. J. Mol. Biol. 254:342-349.
    • (1995) J. Mol. Biol. , vol.254 , pp. 342-349
    • Kimura, M.1    Ishihama, A.2
  • 13
    • 0025767136 scopus 로고
    • Mutations in the three largest subunits of yeast RNA polymerase II that affect enzyme assembly
    • Kolodziej, P. A., and R. A. Young, 1991. Mutations in the three largest subunits of yeast RNA polymerase II that affect enzyme assembly. Mol. Cell. Biol. 11:4669-4678.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4669-4678
    • Kolodziej, P.A.1    Young, R.A.2
  • 14
    • 0344780847 scopus 로고    scopus 로고
    • Functional compartmentalization of the nucleus in the budding yeast Saccharomyces cerevisiae
    • Leger-Silvestre, I., S. Trumtel, J. Noaillac-Depeyre, and N. Gas. 1999. Functional compartmentalization of the nucleus in the budding yeast Saccharomyces cerevisiae. Chromosoma 108:103-113.
    • (1999) Chromosoma , vol.108 , pp. 103-113
    • Leger-Silvestre, I.1    Trumtel, S.2    Noaillac-Depeyre, J.3    Gas, N.4
  • 15
    • 0033568350 scopus 로고    scopus 로고
    • A zinc binding site in the largest subunit of DNA-dependent RNA polymerase is involved in enzyme assembly
    • Markov, D., T. Naryshkina, A. Mustaev, and K. Severinov. 1999. A zinc binding site in the largest subunit of DNA-dependent RNA polymerase is involved in enzyme assembly. Genes Dev. 13:2439-2448.
    • (1999) Genes Dev. , vol.13 , pp. 2439-2448
    • Markov, D.1    Naryshkina, T.2    Mustaev, A.3    Severinov, K.4
  • 16
    • 0026088650 scopus 로고
    • Suppressor analysis of temperature-sensitive RNA polymerase I mutations in Saccharomyces cerevisiae: Suppression of mutations in a zinc-binding motif by transposed mutant genes
    • McCusker, J. H., M. Yamagishi, J. M. Kolb, and M. Nomura. 1991. Suppressor analysis of temperature-sensitive RNA polymerase I mutations in Saccharomyces cerevisiae: suppression of mutations in a zinc-binding motif by transposed mutant genes. Mol. Cell. Biol. 11:746-753.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 746-753
    • McCusker, J.H.1    Yamagishi, M.2    Kolb, J.M.3    Nomura, M.4
  • 17
    • 0035970037 scopus 로고    scopus 로고
    • Bacterial RNA polymerase subunit ω and eukaryotic RNA polymerase subunit RPB6 are sequence, structural, and functional homologs and promote RNA polymerase assembly
    • Minakhin, L., S. Bhagat, A. Brunning, E. A. Campbell, S. A. Darst, R. H. Ebright, and K. Severinov. 2001. Bacterial RNA polymerase subunit ω and eukaryotic RNA polymerase subunit RPB6 are sequence, structural, and functional homologs and promote RNA polymerase assembly. Proc. Natl. Acad. Sci. USA 98:892-897.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 892-897
    • Minakhin, L.1    Bhagat, S.2    Brunning, A.3    Campbell, E.A.4    Darst, S.A.5    Ebright, R.H.6    Severinov, K.7
  • 18
    • 0037123602 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: An RNA polymerase holoenzyme-DNA complex
    • Murakami, K. S., S. Masuda, E. A. Campbell, O. Muzzin, and S. A. Darst. 2002. Structural basis of transcription initiation: an RNA polymerase holoenzyme-DNA complex. Science 296:1285-1290.
    • (2002) Science , vol.296 , pp. 1285-1290
    • Murakami, K.S.1    Masuda, S.2    Campbell, E.A.3    Muzzin, O.4    Darst, S.A.5
  • 19
    • 0034613182 scopus 로고    scopus 로고
    • Inter- and intrasubunit interactions during the formation of RNA polymerase assembly intermediate
    • Naryshkina, T., D. Rogulja, L. Golub, and K. Severinov. 2000. Inter- and intrasubunit interactions during the formation of RNA polymerase assembly intermediate. J. Biol. Chem. 275:31183-31190.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31183-31190
    • Naryshkina, T.1    Rogulja, D.2    Golub, L.3    Severinov, K.4
  • 20
    • 0025797364 scopus 로고
    • Synthesis of large rRNAs by RNA polymerase II in mutants of Saccharomyces cerevisiae defective in RNA polymerase I
    • Nogi, Y., R. Yano, and M. Nomura. 1991. Synthesis of large rRNAs by RNA polymerase II in mutants of Saccharomyces cerevisiae defective in RNA polymerase I. Proc. Natl. Acad. Sci. USA 88:3962-3966
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3962-3966
    • Nogi, Y.1    Yano, R.2    Nomura, M.3
  • 21
    • 0027390138 scopus 로고
    • Gene RRN4 in Saccharomyces cerevisiae encodes the A12.2 subunit of RNA polymerase I and is essential only at high temperatures
    • Nogi, Y., R. Yano, J. Dodd, C. Carles, and M. Nomura. 1993. Gene RRN4 in Saccharomyces cerevisiae encodes the A12.2 subunit of RNA polymerase I and is essential only at high temperatures. Mol. Cell. Biol. 13:114-122.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 114-122
    • Nogi, Y.1    Yano, R.2    Dodd, J.3    Carles, C.4    Nomura, M.5
  • 22
    • 0027477393 scopus 로고
    • Structural alterations of the nucleolus in mutants of Saccharomyces cerevisiae defective in RNA polymerase I
    • Oakes, M., Y. Nogi, M. W. Clark, and M. Nomura. 1993. Structural alterations of the nucleolus in mutants of Saccharomyces cerevisiae defective in RNA polymerase I. Mol. Cell. Biol. 13:2441-2455.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2441-2455
    • Oakes, M.1    Nogi, Y.2    Clark, M.W.3    Nomura, M.4
  • 23
    • 0020490577 scopus 로고
    • Natural variation in yeast RNA polymerase A. Formation of a mosaic RNA polymerase A in a meiotic segregant from an interspecific hybrid
    • Riva, M., J. M. Buhler, A. Sentenac, P. Fromageot, and D. C. Hawthorne. 1982 Natural variation in yeast RNA polymerase A. Formation of a mosaic RNA polymerase A in a meiotic segregant from an interspecific hybrid. J. Biol. Chem. 257:4570-4577
    • (1982) J. Biol. Chem. , vol.257 , pp. 4570-4577
    • Riva, M.1    Buhler, J.M.2    Sentenac, A.3    Fromageot, P.4    Hawthorne, D.C.5
  • 24
    • 0033615355 scopus 로고    scopus 로고
    • Functional characterization of ABC10α, an essential polypeptide shared by all three forms of eukaryotic DNA-dependent RNA polymerases
    • Rubbi, L., S. Labarre-Mariotte, S. Chedin, and P. Thuriaux. 1999. Functional characterization of ABC10α, an essential polypeptide shared by all three forms of eukaryotic DNA-dependent RNA polymerases. J. Biol. Chem. 274:31485-31492.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31485-31492
    • Rubbi, L.1    Labarre-Mariotte, S.2    Chedin, S.3    Thuriaux, P.4
  • 25
    • 0036033732 scopus 로고    scopus 로고
    • Sequence-specific interaction of nascent antiterminator RNA with the zinc-finger motif of Escherichia coli RNA polymerase
    • Sen, R., R. A. King, N. Mzhavia, P. L. Madsen, and R. A. Weisberg. 2002. Sequence-specific interaction of nascent antiterminator RNA with the zinc-finger motif of Escherichia coli RNA polymerase. Mol. Microbiol. 46:215-222.
    • (2002) Mol. Microbiol. , vol.46 , pp. 215-222
    • Sen, R.1    King, R.A.2    Mzhavia, N.3    Madsen, P.L.4    Weisberg, R.A.5
  • 26
    • 0344271983 scopus 로고
    • Prokaryotic and eukaryotic RNA polymerases have homologous core subunits
    • Sweetser, D., M. Nonet, and R. A. Young. 1987. Prokaryotic and eukaryotic RNA polymerases have homologous core subunits. Proc. Natl. Acad. Sci. USA 84:1192-1196.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1192-1196
    • Sweetser, D.1    Nonet, M.2    Young, R.A.3
  • 27
    • 0025788283 scopus 로고
    • Zinc-binding subunits of yeast RNA polymerases
    • Treich, I., M. Riva, and A. Sentenac. 1991. Zinc-binding subunits of yeast RNA polymerases. J. Biol. Chem. 266:21971-21976.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21971-21976
    • Treich, I.1    Riva, M.2    Sentenac, A.3
  • 28
    • 0343081680 scopus 로고    scopus 로고
    • Assembly and functional organization of the nucleolus: Ultrastructural analysis of Saccharomyces cerevisiae mutants
    • Trumtel, S., I. Leger-Silvestre, P. E. Gleizes, F. Teulieres, and N. Gas. 2000. Assembly and functional organization of the nucleolus: ultrastructural analysis of Saccharomyces cerevisiae mutants. Mol. Biol Cell. 11:2175-2189.
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 2175-2189
    • Trumtel, S.1    Leger-Silvestre, I.2    Gleizes, P.E.3    Teulieres, F.4    Gas, N.5
  • 29
    • 0025303335 scopus 로고
    • Zinc coordination, function, and structure of zinc enzymes and other proteins
    • Vallee, B. L., and D. S. Auld. 1990. Zinc coordination, function, and structure of zinc enzymes and other proteins. Biochemistry 29:5647-5659.
    • (1990) Biochemistry , vol.29 , pp. 5647-5659
    • Vallee, B.L.1    Auld, D.S.2
  • 30
    • 0036227539 scopus 로고    scopus 로고
    • Rpa12p, a conserved RNA polymerase I subunit with two functional domains
    • Van Mullein, V., E. Landrieux, J. Vandenhaute, and P. Thuriaux. 2002. Rpa12p, a conserved RNA polymerase I subunit with two functional domains. Mol. Microbiol. 43:1105-1113.
    • (2002) Mol. Microbiol. , vol.43 , pp. 1105-1113
    • Van Mullein, V.1    Landrieux, E.2    Vandenhaute, J.3    Thuriaux, P.4
  • 31
    • 0037155793 scopus 로고    scopus 로고
    • The Rpb9 subunit of RNA polymerase II binds transcription factor TFIIE and interferes with the SAGA and elongator histone acetyltransferases
    • Van Mullein, V., M. Wery, M. Werner, J. Vandenhaute, and P. Thuriaux. 2002. The Rpb9 subunit of RNA polymerase II binds transcription factor TFIIE and interferes with the SAGA and elongator histone acetyltransferases. J. Biol. Chem. 277:10220-10225.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10220-10225
    • Van Mullem, V.1    Wery, M.2    Werner, M.3    Vandenhaute, J.4    Thuriaux, P.5
  • 33
    • 0026590733 scopus 로고
    • Effect of mutations in a zinc-binding domain of yeast RNA polymerase C (III) on enzyme function and subunit association
    • Werner, M., S. Hermann-Le Denmat, I. Treich, A. Sentenac, and P. Thuriaux. 1992. Effect of mutations in a zinc-binding domain of yeast RNA polymerase C (III) on enzyme function and subunit association. Mol. Cell. Biol. 12:1087-1095.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1087-1095
    • Werner, M.1    Hermann-Le Denmat, S.2    Treich, I.3    Sentenac, A.4    Thuriaux, P.5
  • 34
    • 0026068741 scopus 로고
    • Suppressor analysis of temperature-sensitive mutations of the largest subunit of RNA polymerase I in Saccharomyces cerevisiae: A suppressor gene encodes the second-largest subunit of RNA polymerase I
    • Yano, R., and M. Nomura. 1991. Suppressor analysis of temperature-sensitive mutations of the largest subunit of RNA polymerase I in Saccharomyces cerevisiae: a suppressor gene encodes the second-largest subunit of RNA polymerase I. Mol. Cell. Biol. 11:754-764.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 754-764
    • Yano, R.1    Nomura, M.2
  • 35
    • 0026490039 scopus 로고
    • Cloning and characterization of SRP1, a suppressor of temperature-sensitive RNA polymerase I mutations, in Saccharomyces cerevisiae
    • Yano, R., M. Oakes, M. Yamaghishi, J. A. Dodd, and M. Nomura. 1992. Cloning and characterization of SRP1, a suppressor of temperature-sensitive RNA polymerase I mutations, in Saccharomyces cerevisiae. Mol. Cell. Biol. 12:5640-5651.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5640-5651
    • Yano, R.1    Oakes, M.2    Yamaghishi, M.3    Dodd, J.A.4    Nomura, M.5
  • 37
    • 0033578701 scopus 로고    scopus 로고
    • Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution
    • Zhang, G., E. A. Campbell, L. Minakhin, C. Richter, K. Severinov, and S. A. Darst. 1999. Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å 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


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