메뉴 건너뛰기




Volumn 30, Issue 1, 2010, Pages 33-42

Cwc23, an essential J protein critical for pre-mRNA splicing with a dispensable J domain

Author keywords

[No Author keywords available]

Indexed keywords

CWC23 PROTEIN; HEAT SHOCK PROTEIN 70; MESSENGER RNA; NTR1 PROTEIN; PROTEIN; PROTEIN DERIVATIVE; PRP43 PROTEIN; UNCLASSIFIED DRUG;

EID: 73549123446     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.00842-09     Document Type: Article
Times cited : (36)

References (44)
  • 1
    • 0033200012 scopus 로고    scopus 로고
    • G-patch: A new conserved domain in eukaryotic RNA-processing proteins and type D retroviral polyproteins
    • Aravind, L., and E. V. Koonin. 1999. G-patch: a new conserved domain in eukaryotic RNA-processing proteins and type D retroviral polyproteins. Trends Biochem. Sci. 24:342-344.
    • (1999) Trends Biochem. Sci , vol.24 , pp. 342-344
    • Aravind, L.1    Koonin, E.V.2
  • 2
    • 0030671163 scopus 로고    scopus 로고
    • Prp43: An RNA helicase-like factor involved in spliceosome disassembly
    • Arenas, J. E., and J. N. Abelson. 1997. Prp43: an RNA helicase-like factor involved in spliceosome disassembly. Proc. Natl. Acad. Sci. USA 94:11798-11802.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11798-11802
    • Arenas, J.E.1    Abelson, J.N.2
  • 3
    • 34548101963 scopus 로고    scopus 로고
    • J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation
    • Aron, R., T. Higurashi, C. Sahi, and E. A. Craig. 2007. J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation. EMBO J. 26:3794-3803.
    • (2007) EMBO J , vol.26 , pp. 3794-3803
    • Aron, R.1    Higurashi, T.2    Sahi, C.3    Craig, E.A.4
  • 5
    • 0036948420 scopus 로고    scopus 로고
    • Allosteric cascade of spliceosome activation
    • Brow, D. A. 2002. Allosteric cascade of spliceosome activation. Annu. Rev. Genet. 36:333-360.
    • (2002) Annu. Rev. Genet , vol.36 , pp. 333-360
    • Brow, D.A.1
  • 6
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau, B., J. Weissman, and A. Horwich. 2006. Molecular chaperones and protein quality control. Cell 125:443-451.
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 10
    • 0029670585 scopus 로고    scopus 로고
    • Mutations in the RNA polymerase II transcription machinery suppress the hyperrecombination mutant hpr1Δ of Saccharomyces cerevisiae
    • Fan, H. Y., K. K. Cheng, and H. L. Klein. 1996. Mutations in the RNA polymerase II transcription machinery suppress the hyperrecombination mutant hpr1Δ of Saccharomyces cerevisiae. Genetics 142:749-759.
    • (1996) Genetics , vol.142 , pp. 749-759
    • Fan, H.Y.1    Cheng, K.K.2    Klein, H.L.3
  • 11
    • 17844395704 scopus 로고    scopus 로고
    • Prp8 protein: At the heart of the spliceosome
    • Grainger, R. J., and J. D. Beggs. 2005. Prp8 protein: at the heart of the spliceosome. RNA 11:533-557.
    • (2005) RNA , vol.11 , pp. 533-557
    • Grainger, R.J.1    Beggs, J.D.2
  • 12
    • 0032568541 scopus 로고    scopus 로고
    • Role of the J-domain in the cooperation of Hsp40 with Hsp70
    • Greene, M. K., K. Maskos, and S. J. Landry. 1998. Role of the J-domain in the cooperation of Hsp40 with Hsp70. Proc. Natl. Acad. Sci. USA 95:6108-6113.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6108-6113
    • Greene, M.K.1    Maskos, K.2    Landry, S.J.3
  • 13
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F. U., and M. Hayer-Hartl. 2002. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295:1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 14
    • 22344447035 scopus 로고    scopus 로고
    • Hennessy, F., W. S. Nicoll, R. Zimmermann, M. E. Cheetham, and G. L. Blatch. 2005. Not all J. domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions. Protein Sci. 14:1697-1709.
    • Hennessy, F., W. S. Nicoll, R. Zimmermann, M. E. Cheetham, and G. L. Blatch. 2005. Not all J. domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions. Protein Sci. 14:1697-1709.
  • 15
    • 22444439361 scopus 로고    scopus 로고
    • The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1
    • Huang, P., M. Gautschi, W. Walter, S. Rospert, and E. A. Craig. 2005. The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1. Nat. Struct. Mol. Biol. 12:497-504.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 497-504
    • Huang, P.1    Gautschi, M.2    Walter, W.3    Rospert, S.4    Craig, E.A.5
  • 16
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
    • James, P., J. Halladay, and E. A. Craig. 1996. Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics 144:1425-1436.
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2    Craig, E.A.3
  • 17
    • 35649024724 scopus 로고    scopus 로고
    • Jiang, J., E. G. Maes, A. B. Taylor, L. Wang, A. P. Hinck, E. M. Lafer, and R. Sousa. 2007. Structural basis of J cochaperone binding and regulation of Hsp70. Mol. Cell 28:422-433.
    • Jiang, J., E. G. Maes, A. B. Taylor, L. Wang, A. P. Hinck, E. M. Lafer, and R. Sousa. 2007. Structural basis of J cochaperone binding and regulation of Hsp70. Mol. Cell 28:422-433.
  • 18
    • 0034005058 scopus 로고    scopus 로고
    • A role for the Hsp40 Ydj1 in repression of basal steroid receptor activity in yeast
    • Johnson, J. L., and E. A. Craig. 2000. A role for the Hsp40 Ydj1 in repression of basal steroid receptor activity in yeast. Mol. Cell. Biol. 20:3027-3036.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 3027-3036
    • Johnson, J.L.1    Craig, E.A.2
  • 20
    • 0037418880 scopus 로고    scopus 로고
    • Regulated cycling of mitochondrial Hsp70 at the protein import channel
    • Liu, Q., P. D'Silva, W. Walter, J. Marszalek, and E. A. Craig. 2003. Regulated cycling of mitochondrial Hsp70 at the protein import channel. Science 300:139-141.
    • (2003) Science , vol.300 , pp. 139-141
    • Liu, Q.1    D'Silva, P.2    Walter, W.3    Marszalek, J.4    Craig, E.A.5
  • 21
    • 0032417527 scopus 로고    scopus 로고
    • The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains
    • Lopez-Buesa, P., C. Pfund, and E. A. Craig. 1998. The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains. Proc. Natl. Acad. Sci. USA 95:15253-15258.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15253-15258
    • Lopez-Buesa, P.1    Pfund, C.2    Craig, E.A.3
  • 22
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux, B., and J. E. Walker. 1996. Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260:289-298.
    • (1996) J. Mol. Biol , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 23
    • 0028953840 scopus 로고
    • Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds
    • Mumberg, D., R. Muller, and M. Funk. 1995. Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds. Gene 156:119-122.
    • (1995) Gene , vol.156 , pp. 119-122
    • Mumberg, D.1    Muller, R.2    Funk, M.3
  • 24
    • 0344198459 scopus 로고    scopus 로고
    • The spliceosome: The most complex macromolecular machine in the cell?
    • Nilsen, T. W. 2003. The spliceosome: the most complex macromolecular machine in the cell? Bioessays 25:1147-1149.
    • (2003) Bioessays , vol.25 , pp. 1147-1149
    • Nilsen, T.W.1
  • 25
    • 0036118353 scopus 로고    scopus 로고
    • Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs
    • Ohi, M. D., A. J. Link, L. Ren, J. L. Jennings, W. H. McDonald, and K. L. Gould. 2002. Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs. Mol. Cell. Biol. 22:2011-2024.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 2011-2024
    • Ohi, M.D.1    Link, A.J.2    Ren, L.3    Jennings, J.L.4    McDonald, W.H.5    Gould, K.L.6
  • 26
    • 33748766359 scopus 로고    scopus 로고
    • Inhibition of a spliceosome turnover pathway suppresses splicing defects
    • Pandit, S., B. Lynn, and B. C. Rymond. 2006. Inhibition of a spliceosome turnover pathway suppresses splicing defects. Proc. Natl. Acad. Sci. USA 103:13700-13705.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13700-13705
    • Pandit, S.1    Lynn, B.2    Rymond, B.C.3
  • 27
    • 55549141494 scopus 로고    scopus 로고
    • Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3
    • Petrova, K., S. Oyadomari, L. M. Hendershot, and D. Ron. 2008. Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3. EMBO J. 27:2862-2872.
    • (2008) EMBO J , vol.27 , pp. 2862-2872
    • Petrova, K.1    Oyadomari, S.2    Hendershot, L.M.3    Ron, D.4
  • 28
    • 0035658334 scopus 로고    scopus 로고
    • Divergent functional properties of the ribosome-associated molecular chaperone Ssb compared with other Hsp70s
    • Pfund, C., P. Huang, N. Lopez-Hoyo, and E. A. Craig. 2001. Divergent functional properties of the ribosome-associated molecular chaperone Ssb compared with other Hsp70s. Mol. Biol. Cell 12:3773-3782.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3773-3782
    • Pfund, C.1    Huang, P.2    Lopez-Hoyo, N.3    Craig, E.A.4
  • 29
    • 34247255773 scopus 로고    scopus 로고
    • Transcript specificity in yeast pre-mRNA splicing revealed by mutations in core spliceosomal components
    • Pleiss, J. A., G. B. Whitworth, M. Bergkessel, and C. Guthrie. 2007. Transcript specificity in yeast pre-mRNA splicing revealed by mutations in core spliceosomal components. PLoS Biol. 5:e90.
    • (2007) PLoS Biol , vol.5
    • Pleiss, J.A.1    Whitworth, G.B.2    Bergkessel, M.3    Guthrie, C.4
  • 30
    • 33644847698 scopus 로고    scopus 로고
    • The evolution of spliceosomal introns: Patterns, puzzles and progress
    • Roy, S. W., and W. Gilbert. 2006. The evolution of spliceosomal introns: patterns, puzzles and progress. Nat. Rev. Genet. 7:211-221.
    • (2006) Nat. Rev. Genet , vol.7 , pp. 211-221
    • Roy, S.W.1    Gilbert, W.2
  • 31
    • 34249853249 scopus 로고    scopus 로고
    • Sahi, C., and E. A. Craig. 2007. Network of general and specialty J. protein chaperones of the yeast cytosol. Proc. Natl. Acad. Sci. USA 104:7163-7168.
    • Sahi, C., and E. A. Craig. 2007. Network of general and specialty J. protein chaperones of the yeast cytosol. Proc. Natl. Acad. Sci. USA 104:7163-7168.
  • 33
    • 34548842257 scopus 로고    scopus 로고
    • Ntr1 activates the Prp43 helicase to trigger release of lariat-intron from the spliceosome
    • Tanaka, N., A. Aronova, and B. Schwer. 2007. Ntr1 activates the Prp43 helicase to trigger release of lariat-intron from the spliceosome. Genes Dev. 21:2312-2325.
    • (2007) Genes Dev , vol.21 , pp. 2312-2325
    • Tanaka, N.1    Aronova, A.2    Schwer, B.3
  • 34
    • 0345390061 scopus 로고    scopus 로고
    • Disruption of six novel Saccharomyces cerevisiae genes reveals that YGL129c is necessary for growth in non-fermentable carbon sources, YGL128c for growth at low or high temperatures and YGL125w is implicated in the biosynthesis of methionine
    • Tizon, B., A. M. Rodriguez-Torres, and M. E. Cerdan. 1999. Disruption of six novel Saccharomyces cerevisiae genes reveals that YGL129c is necessary for growth in non-fermentable carbon sources, YGL128c for growth at low or high temperatures and YGL125w is implicated in the biosynthesis of methionine. Yeast 15:145-154.
    • (1999) Yeast , vol.15 , pp. 145-154
    • Tizon, B.1    Rodriguez-Torres, A.M.2    Cerdan, M.E.3
  • 35
    • 29144515824 scopus 로고    scopus 로고
    • Spliceosome disassembly catalyzed by Prp43 and its associated components Ntr1 and Ntr2
    • Tsai, R. T., R. H. Fu, F. L. Yeh, C. K. Tseng, Y. C. Lin, Y. H. Huang, and S. C. Cheng. 2005. Spliceosome disassembly catalyzed by Prp43 and its associated components Ntr1 and Ntr2. Genes Dev. 19:2991-3003.
    • (2005) Genes Dev , vol.19 , pp. 2991-3003
    • Tsai, R.T.1    Fu, R.H.2    Yeh, F.L.3    Tseng, C.K.4    Lin, Y.C.5    Huang, Y.H.6    Cheng, S.C.7
  • 36
    • 36849009618 scopus 로고    scopus 로고
    • Dynamic interactions of Ntr1-Ntr2 with Prp43 and with U5 govern the recruitment of Prp43 to mediate spliceosome disassembly
    • Tsai, R. T., C. K. Tseng, P. J. Lee, H. C. Chen, R. H. Fu, K. J. Chang, F. L. Yeh, and S. C. Cheng. 2007. Dynamic interactions of Ntr1-Ntr2 with Prp43 and with U5 govern the recruitment of Prp43 to mediate spliceosome disassembly. Mol. Cell. Biol. 27:8027-8037.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 8027-8037
    • Tsai, R.T.1    Tseng, C.K.2    Lee, P.J.3    Chen, H.C.4    Fu, R.H.5    Chang, K.J.6    Yeh, F.L.7    Cheng, S.C.8
  • 37
    • 0042195847 scopus 로고    scopus 로고
    • New 'marker swap' plasmids for converting selectable markers on budding yeast gene disruptions and plasmids
    • Voth, W. P., Y. W. Jiang, and D. J. Stillman. 2003. New 'marker swap' plasmids for converting selectable markers on budding yeast gene disruptions and plasmids. Yeast 20:985-993.
    • (2003) Yeast , vol.20 , pp. 985-993
    • Voth, W.P.1    Jiang, Y.W.2    Stillman, D.J.3
  • 38
    • 60349104299 scopus 로고    scopus 로고
    • The spliceosome: Design principles of a dynamic RNP machine
    • Wahl, M. C., C. L. Will, and R. Luhrmann. 2009. The spliceosome: design principles of a dynamic RNP machine. Cell 136:701-718.
    • (2009) Cell , vol.136 , pp. 701-718
    • Wahl, M.C.1    Will, C.L.2    Luhrmann, R.3
  • 39
    • 4344590764 scopus 로고    scopus 로고
    • The J-protein family: Modulating protein assembly, disassembly, and translocation
    • Walsh, P., D. Bursac, Y. C. Law, D. Cyr, and T. Lithgow. 2004. The J-protein family: modulating protein assembly, disassembly, and translocation. EMBO Rep. 5:567-571.
    • (2004) EMBO Rep , vol.5 , pp. 567-571
    • Walsh, P.1    Bursac, D.2    Law, Y.C.3    Cyr, D.4    Lithgow, T.5
  • 40
    • 0033529707 scopus 로고    scopus 로고
    • Winzeler, E. A, D. D. Shoemaker, A. Astromoff, H. Liang, K. Anderson, B. Andre, R. Bangham, R. Benito, J. D. Boeke, H. Bussey, A. M. Chu, C. Connelly, K. Davis, F. Dietrich, S. W. Dow, M. El Bakkoury, F. Foury, S. H. Friend, E. Gentalen, G. Giaever, J. H. Hegemann, T. Jones, M. Laub, H. Liao, N. Liebundguth, D. J. Lockhart, A. Lucau-Danila, M. Lussier, N. M'Rabet, P. Menard, M. Mittmann, C. Pai, C. Rebischung, J. L. Revuelta, L. Riles, C. J. Roberts, P. Ross-MacDonald, B. Scherens, M. Snyder, S. Sookhai-Mahadeo, R. K. Storms, S. Veronneau, M. Voet, G. Volckaert, T. R. Ward, R. Wysocki, G. S. Yen, K. Yu, K. Zimmermann, P. Philippsen, M. Johnston, and R. W. Davis. 1999. Functional characterization of the Saccharomyces cerevisiae genome by gene deletion and parallel analysis. Science 285:901-906
    • Winzeler, E. A., D. D. Shoemaker, A. Astromoff, H. Liang, K. Anderson, B. Andre, R. Bangham, R. Benito, J. D. Boeke, H. Bussey, A. M. Chu, C. Connelly, K. Davis, F. Dietrich, S. W. Dow, M. El Bakkoury, F. Foury, S. H. Friend, E. Gentalen, G. Giaever, J. H. Hegemann, T. Jones, M. Laub, H. Liao, N. Liebundguth, D. J. Lockhart, A. Lucau-Danila, M. Lussier, N. M'Rabet, P. Menard, M. Mittmann, C. Pai, C. Rebischung, J. L. Revuelta, L. Riles, C. J. Roberts, P. Ross-MacDonald, B. Scherens, M. Snyder, S. Sookhai-Mahadeo, R. K. Storms, S. Veronneau, M. Voet, G. Volckaert, T. R. Ward, R. Wysocki, G. S. Yen, K. Yu, K. Zimmermann, P. Philippsen, M. Johnston, and R. W. Davis. 1999. Functional characterization of the Saccharomyces cerevisiae genome by gene deletion and parallel analysis. Science 285:901-906.
  • 41
    • 0032694248 scopus 로고    scopus 로고
    • The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 Sis1
    • Yan, W., and E. A. Craig. 1999. The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 Sis1. Mol. Cell. Biol. 19:7751-7758.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 7751-7758
    • Yan, W.1    Craig, E.A.2
  • 42
    • 0037117746 scopus 로고    scopus 로고
    • Yan, W., M. J. Gale, Jr., S. L. Tan, and M. G. Katze. 2002. Inactivation of the PKR protein kinase and stimulation of mRNA translation by the cellular co-chaperone P58(IPK) does not require J. domain function. Biochemistry 41:4938-4945.
    • Yan, W., M. J. Gale, Jr., S. L. Tan, and M. G. Katze. 2002. Inactivation of the PKR protein kinase and stimulation of mRNA translation by the cellular co-chaperone P58(IPK) does not require J. domain function. Biochemistry 41:4938-4945.
  • 43
    • 0032541489 scopus 로고    scopus 로고
    • Zuotin, a ribosome-associated DnaJ molecular chaperone
    • Yan, W., B. Schilke, C. Pfund, W. Walter, S. Kim, and E. A. Craig. 1998. Zuotin, a ribosome-associated DnaJ molecular chaperone. EMBO J. 17: 4809-4817.
    • (1998) EMBO J , vol.17 , pp. 4809-4817
    • Yan, W.1    Schilke, B.2    Pfund, C.3    Walter, W.4    Kim, S.5    Craig, E.A.6
  • 44
    • 38749101566 scopus 로고    scopus 로고
    • Dimeric heat shock protein 40 binds radial spokes for generating coupled power strokes and recovery strokes of 9 2 flagella
    • Yang, C., H. A. Owen, and P. Yang. 2008. Dimeric heat shock protein 40 binds radial spokes for generating coupled power strokes and recovery strokes of 9 2 flagella. J. Cell Biol. 180:403-415.
    • (2008) J. Cell Biol , vol.180 , pp. 403-415
    • Yang, C.1    Owen, H.A.2    Yang, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.