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Volumn 42, Issue 8, 2014, Pages 5343-5358

Sumoylation of the THO complex regulates the biogenesis of a subset of mRNPs

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; MUTANT PROTEIN; PROTEIN HPR1; REGULATOR PROTEIN; THO COMPLEX; UNCLASSIFIED DRUG; CYSTEINE PROTEINASE; EXOSOME MULTIENZYME RIBONUCLEASE COMPLEX; HPR1 PROTEIN, S CEREVISIAE; MESSENGER RIBONUCLEOPROTEIN; NUCLEAR PROTEIN; PROTEOME; RIBONUCLEOPROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; SUMO 1 PROTEIN; ULP1 PROTEASE;

EID: 84899849700     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gku124     Document Type: Article
Times cited : (42)

References (72)
  • 1
    • 84875229872 scopus 로고    scopus 로고
    • How cells get the message: Dynamic assembly and function of mRNA-protein complexes
    • Muller-McNicoll, M. and Neugebauer, K.M. (2013) How cells get the message: dynamic assembly and function of mRNA-protein complexes. Nat. Rev. Genet., 14, 275-287.
    • (2013) Nat. Rev. Genet. , vol.14 , pp. 275-287
    • Muller-Mcnicoll, M.1    Neugebauer, K.M.2
  • 2
    • 84860443663 scopus 로고    scopus 로고
    • New clues to understand the role of THO and other functionally related factors in mRNP biogenesis
    • Luna, R., Rondon, A.G. and Aguilera, A. (2012) New clues to understand the role of THO and other functionally related factors in mRNP biogenesis. Biochim. Biophys. Acta., 1819, 514-520.
    • (2012) Biochim. Biophys. Acta. , vol.1819 , pp. 514-520
    • Luna, R.1    Rondon, A.G.2    Aguilera, A.3
  • 3
    • 84860450204 scopus 로고    scopus 로고
    • To the pore and through the pore: A story of mRNA export kinetics
    • Oeffinger, M. and Zenklusen, D. (2012) To the pore and through the pore: A story of mRNA export kinetics. Biochim. Biophys. Acta., 1819, 494-506.
    • (2012) Biochim. Biophys. Acta. , vol.1819 , pp. 494-506
    • Oeffinger, M.1    Zenklusen, D.2
  • 4
    • 0034329461 scopus 로고    scopus 로고
    • A protein complex containing Tho2, Hpr1, Mft1 and a novel protein, Thp2, connects transcription elongation with mitotic recombination in Saccharomyces cerevisiae
    • Chavez, S., Beilharz, T., Rondon, A.G., Erdjument-Bromage, H., Tempst, P., Svejstrup, J.Q., Lithgow, T. and Aguilera, A. (2000) A protein complex containing Tho2, Hpr1, Mft1 and a novel protein, Thp2, connects transcription elongation with mitotic recombination in Saccharomyces cerevisiae. EMBO J., 19, 5824-5834.
    • (2000) EMBO J. , vol.19 , pp. 5824-5834
    • Chavez, S.1    Beilharz, T.2    Rondon, A.G.3    Erdjument-Bromage, H.4    Tempst, P.5    Svejstrup, J.Q.6    Lithgow, T.7    Aguilera, A.8
  • 6
    • 0036889334 scopus 로고    scopus 로고
    • Stable mRNP formation and export require cotranscriptional recruitment of the mRNA export factors Yra1p and Sub2p by Hpr1p
    • Zenklusen, D., Vinciguerra, P., Wyss, J.C. and Stutz, F. (2002) Stable mRNP formation and export require cotranscriptional recruitment of the mRNA export factors Yra1p and Sub2p by Hpr1p. Mol. Cell Biol., 22, 8241-8253.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 8241-8253
    • Zenklusen, D.1    Vinciguerra, P.2    Wyss, J.C.3    Stutz, F.4
  • 8
    • 1242319345 scopus 로고    scopus 로고
    • Cotranscriptional recruitment of the serine-arginine-rich (SR)-like proteins Gbp2 and Hrb1 to nascent mRNA via the TREX complex
    • Hurt, E., Luo, M.J., Rother, S., Reed, R. and Strasser, K. (2004) Cotranscriptional recruitment of the serine-arginine-rich (SR)-like proteins Gbp2 and Hrb1 to nascent mRNA via the TREX complex. Proc. Natl Acad. Sci. USA, 101, 1858-1862.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 1858-1862
    • Hurt, E.1    Luo, M.J.2    Rother, S.3    Reed, R.4    Strasser, K.5
  • 9
    • 1242272135 scopus 로고    scopus 로고
    • Differential export requirements for shuttling serine/arginine-type mRNA-binding proteins
    • Hacker, S. and Krebber, H. (2004) Differential export requirements for shuttling serine/arginine-type mRNA-binding proteins. J. Biol. Chem., 279, 5049-5052.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5049-5052
    • Hacker, S.1    Krebber, H.2
  • 12
    • 84855286267 scopus 로고    scopus 로고
    • Genome instability and transcription elongation impairment in human cells depleted of THO/TREX
    • Dominguez-Sanchez, M.S., Barroso, S., Gomez-Gonzalez, B., Luna, R. and Aguilera, A. (2011) Genome instability and transcription elongation impairment in human cells depleted of THO/TREX. PLoS Genet., 7, e1002386.
    • (2011) PLoS Genet. , vol.7
    • Dominguez-Sanchez, M.S.1    Barroso, S.2    Gomez-Gonzalez, B.3    Luna, R.4    Aguilera, A.5
  • 13
    • 0036889142 scopus 로고    scopus 로고
    • Interactions between mRNA export commitment, 3′-end quality control, and nuclear degradation
    • Libri, D., Dower, K., Boulay, J., Thomsen, R., Rosbash, M. and Jensen, T.H. (2002) Interactions between mRNA export commitment, 3′-end quality control, and nuclear degradation. Mol. Cell Biol., 22, 8254-8266.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 8254-8266
    • Libri, D.1    Dower, K.2    Boulay, J.3    Thomsen, R.4    Rosbash, M.5    Jensen, T.H.6
  • 15
    • 18144376727 scopus 로고    scopus 로고
    • Human hHpr1/p84/Thoc1 regulates transcriptional elongation and physically links RNA polymerase II and RNA processing factors
    • Li, Y., Wang, X., Zhang, X. and Goodrich, D.W. (2005) Human hHpr1/p84/Thoc1 regulates transcriptional elongation and physically links RNA polymerase II and RNA processing factors. Mol. Cell Biol., 25, 4023-4033.
    • (2005) Mol. Cell Biol. , vol.25 , pp. 4023-4033
    • Li, Y.1    Wang, X.2    Zhang, X.3    Goodrich, D.W.4
  • 18
    • 0036645687 scopus 로고    scopus 로고
    • The yeast THO complex and mRNA export factors link RNA metabolism with transcription and genome instability
    • Jimeno, S., Rondon, A.G., Luna, R. and Aguilera, A. (2002) The yeast THO complex and mRNA export factors link RNA metabolism with transcription and genome instability. EMBO J., 21, 3526-3535.
    • (2002) EMBO J. , vol.21 , pp. 3526-3535
    • Jimeno, S.1    Rondon, A.G.2    Luna, R.3    Aguilera, A.4
  • 19
    • 0141819093 scopus 로고    scopus 로고
    • Cotranscriptionally formed DNA:RNA hybrids mediate transcription elongation impairment and transcription-associated recombination
    • Huertas, P. and Aguilera, A. (2003) Cotranscriptionally formed DNA:RNA hybrids mediate transcription elongation impairment and transcription-associated recombination. Mol. Cell, 12, 711-721.
    • (2003) Mol. Cell , vol.12 , pp. 711-721
    • Huertas, P.1    Aguilera, A.2
  • 21
    • 67650492477 scopus 로고    scopus 로고
    • Mechanisms of nuclear mRNA quality control
    • Fasken, M.B. and Corbett, A.H. (2009) Mechanisms of nuclear mRNA quality control. RNA Biol., 6, 237-241.
    • (2009) RNA Biol. , vol.6 , pp. 237-241
    • Fasken, M.B.1    Corbett, A.H.2
  • 22
    • 84872396711 scopus 로고    scopus 로고
    • Transcription-associated quality control of mRNP
    • Schmid, M. and Jensen, T.H. (2013) Transcription-associated quality control of mRNP. Biochim. Biophys. Acta., 1829, 158-168.
    • (2013) Biochim. Biophys. Acta. , vol.1829 , pp. 158-168
    • Schmid, M.1    Jensen, T.H.2
  • 23
    • 84857590342 scopus 로고    scopus 로고
    • Dbp5, Gle1-IP6, and Nup159: A working model for mRNP export
    • Folkmann, A.W., Noble, K.N., Cole, C.N. and Wente, S.R. (2011) Dbp5, Gle1-IP6, and Nup159: a working model for mRNP export. Nucleus, 2, 540-548.
    • (2011) Nucleus , vol.2 , pp. 540-548
    • Folkmann, A.W.1    Noble, K.N.2    Cole, C.N.3    Wente, S.R.4
  • 24
    • 0035846109 scopus 로고    scopus 로고
    • Splicing factor Sub2p is required for nuclear mRNA export through its interaction with Yra1p
    • Strasser, K. and Hurt, E. (2001) Splicing factor Sub2p is required for nuclear mRNA export through its interaction with Yra1p. Nature, 413, 648-652.
    • (2001) Nature , vol.413 , pp. 648-652
    • Strasser, K.1    Hurt, E.2
  • 26
    • 79957496447 scopus 로고    scopus 로고
    • Keeping mRNPs in check during assembly and nuclear export
    • Tutucci, E. and Stutz, F. (2011) Keeping mRNPs in check during assembly and nuclear export. Nat. Rev. Mol. Cell Biol., 12, 377-384.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 377-384
    • Tutucci, E.1    Stutz, F.2
  • 29
    • 84860443753 scopus 로고    scopus 로고
    • Emerging roles for SUMO in mRNA processing and metabolism
    • Springer, Dordrecht
    • Vethantham, V. and Manley, J.L. (2009) Emerging roles for SUMO in mRNA processing and metabolism. In SUMO Regulation of Cellular Processes. Springer, Dordrecht, pp. 41-57.
    • (2009) SUMO Regulation of Cellular Processes , pp. 41-57
    • Vethantham, V.1    Manley, J.L.2
  • 30
    • 84885870186 scopus 로고    scopus 로고
    • Multiple crosstalks between mRNA biogenesis and SUMO
    • Rouviere, J.O., Geoffroy, M.C. and Palancade, B. (2013) Multiple crosstalks between mRNA biogenesis and SUMO. Chromosoma, 122, 387-399.
    • (2013) Chromosoma , vol.122 , pp. 387-399
    • Rouviere, J.O.1    Geoffroy, M.C.2    Palancade, B.3
  • 31
    • 78649396592 scopus 로고    scopus 로고
    • The SUMO pathway: Emerging mechanisms that shape specificity, conjugation and recognition
    • Gareau, J.R. and Lima, C.D. (2010) The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nat. Rev. Mol. Cell Biol., 11, 861-871.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 32
    • 0037417959 scopus 로고    scopus 로고
    • The C-terminal domain of myosin-like protein 1 (Mlp1p) is a docking site for heterogeneous nuclear ribonucleoproteins that are required for mRNA export
    • Green, D.M., Johnson, C.P., Hagan, H. and Corbett, A.H. (2003) The C-terminal domain of myosin-like protein 1 (Mlp1p) is a docking site for heterogeneous nuclear ribonucleoproteins that are required for mRNA export. Proc. Natl Acad. Sci. USA, 100, 1010-1015.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 1010-1015
    • Green, D.M.1    Johnson, C.P.2    Hagan, H.3    Corbett, A.H.4
  • 33
    • 15444368318 scopus 로고    scopus 로고
    • Perinuclear Mlp proteins downregulate gene expression in response to a defect in mRNA export
    • Vinciguerra, P., Iglesias, N., Camblong, J., Zenklusen, D. and Stutz, F. (2005) Perinuclear Mlp proteins downregulate gene expression in response to a defect in mRNA export. EMBO J., 24, 813-823.
    • (2005) EMBO J. , vol.24 , pp. 813-823
    • Vinciguerra, P.1    Iglesias, N.2    Camblong, J.3    Zenklusen, D.4    Stutz, F.5
  • 34
    • 9444259173 scopus 로고    scopus 로고
    • Mlp-dependent anchorage and stabilization of a desumoylating enzyme is required to prevent clonal lethality
    • Zhao, X., Wu, C.Y. and Blobel, G. (2004) Mlp-dependent anchorage and stabilization of a desumoylating enzyme is required to prevent clonal lethality. J. Cell Biol., 167, 605-611.
    • (2004) J. Cell Biol. , vol.167 , pp. 605-611
    • Zhao, X.1    Wu, C.Y.2    Blobel, G.3
  • 35
    • 41149157334 scopus 로고    scopus 로고
    • Sumoylating and desumoylating enzymes at nuclear pores: Underpinning their unexpected duties?
    • Palancade, B. and Doye, V. (2008) Sumoylating and desumoylating enzymes at nuclear pores: underpinning their unexpected duties? Trends Cell Biol., 18, 174-183.
    • (2008) Trends Cell Biol. , vol.18 , pp. 174-183
    • Palancade, B.1    Doye, V.2
  • 36
    • 25844432253 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae adaptation to weak acids involves the transcription factor Haa1p and Haa1p-regulated genes
    • Fernandes, A.R., Mira, N.P., Vargas, R.C., Canelhas, I. and Sa-Correia, I. (2005) Saccharomyces cerevisiae adaptation to weak acids involves the transcription factor Haa1p and Haa1p-regulated genes. Biochem. Biophys. Res. Commun., 337, 95-103.
    • (2005) Biochem. Biophys. Res. Commun. , vol.337 , pp. 95-103
    • Fernandes, A.R.1    Mira, N.P.2    Vargas, R.C.3    Canelhas, I.4    Sa-Correia, I.5
  • 40
    • 3343003673 scopus 로고    scopus 로고
    • Biochemical analysis of TREX complex recruitment to intronless and intron-containing yeast genes
    • Abruzzi, K.C., Lacadie, S. and Rosbash, M. (2004) Biochemical analysis of TREX complex recruitment to intronless and intron-containing yeast genes. EMBO J., 23, 2620-2631.
    • (2004) EMBO J. , vol.23 , pp. 2620-2631
    • Abruzzi, K.C.1    Lacadie, S.2    Rosbash, M.3
  • 42
    • 59249091313 scopus 로고    scopus 로고
    • In vivo detection and characterization of sumoylation targets in Saccharomyces cerevisiae
    • Ulrich, H.D. and Davies, A.A. (2009) In vivo detection and characterization of sumoylation targets in Saccharomyces cerevisiae. Methods Mol. Biol., 497, 81-103.
    • (2009) Methods Mol. Biol. , vol.497 , pp. 81-103
    • Ulrich, H.D.1    Davies, A.A.2
  • 43
    • 77954126191 scopus 로고    scopus 로고
    • Teolenn: An efficient and customizable workflow to design high-quality probes for microarray experiments
    • Jourdren, L., Duclos, A., Brion, C., Portnoy, T., Mathis, H., Margeot, A. and Le Crom, S. (2010) Teolenn: an efficient and customizable workflow to design high-quality probes for microarray experiments. Nucleic Acids Res., 38, e117.
    • (2010) Nucleic Acids Res. , vol.38
    • Jourdren, L.1    Duclos, A.2    Brion, C.3    Portnoy, T.4    Mathis, H.5    Margeot, A.6    Le Crom, S.7
  • 44
    • 33750474083 scopus 로고    scopus 로고
    • Goulphar: Rapid access and expertise for standard two-color microarray normalization methods
    • Lemoine, S., Combes, F., Servant, N. and Le Crom, S. (2006) Goulphar: rapid access and expertise for standard two-color microarray normalization methods. BMC Bioinform., 7, 467.
    • (2006) BMC Bioinform. , vol.7 , pp. 467
    • Lemoine, S.1    Combes, F.2    Servant, N.3    Le Crom, S.4
  • 46
    • 0029820765 scopus 로고    scopus 로고
    • Mutations in the yeast SRB2 general transcription factor suppress hpr1-induced recombination and show defects in DNA repair
    • Piruat, J.I. and Aguilera, A. (1996) Mutations in the yeast SRB2 general transcription factor suppress hpr1-induced recombination and show defects in DNA repair. Genetics, 143, 1533-1542.
    • (1996) Genetics , vol.143 , pp. 1533-1542
    • Piruat, J.I.1    Aguilera, A.2
  • 47
    • 34548318654 scopus 로고    scopus 로고
    • A nuclear envelope protein linking nuclear pore basket assembly, SUMO protease regulation, and mRNA surveillance
    • Lewis, A., Felberbaum, R. and Hochstrasser, M. (2007) A nuclear envelope protein linking nuclear pore basket assembly, SUMO protease regulation, and mRNA surveillance. J. Cell Biol., 178, 813-827.
    • (2007) J. Cell Biol. , vol.178 , pp. 813-827
    • Lewis, A.1    Felberbaum, R.2    Hochstrasser, M.3
  • 48
    • 22944465779 scopus 로고    scopus 로고
    • The nuclear pore complex-associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly
    • Niepel, M., Strambio-de-Castillia, C., Fasolo, J., Chait, B.T. and Rout, M.P. (2005) The nuclear pore complex-associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly. J. Cell Biol., 170, 225-235.
    • (2005) J. Cell Biol. , vol.170 , pp. 225-235
    • Niepel, M.1    Strambio-De-Castillia, C.2    Fasolo, J.3    Chait, B.T.4    Rout, M.P.5
  • 53
    • 70350543964 scopus 로고    scopus 로고
    • SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple nonconsensus sites within the B domain and is linked to its activity cycle
    • Figueroa-Romero, C., Iniguez-Lluhi, J.A., Stadler, J., Chang, C.R., Arnoult, D., Keller, P.J., Hong, Y., Blackstone, C. and Feldman, E.L. (2009) SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple nonconsensus sites within the B domain and is linked to its activity cycle. FASEB J., 23, 3917-3927.
    • (2009) FASEB J. , vol.23 , pp. 3917-3927
    • Figueroa-Romero, C.1    Iniguez-Lluhi, J.A.2    Stadler, J.3    Chang, C.R.4    Arnoult, D.5    Keller, P.J.6    Hong, Y.7    Blackstone, C.8    Feldman, E.L.9
  • 55
    • 33847783298 scopus 로고    scopus 로고
    • Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins
    • Xie, H., Vucetic, S., Iakoucheva, L.M., Oldfield, C.J., Dunker, A.K., Obradovic, Z. and Uversky, V.N. (2007) Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins. J. Proteome Res., 6, 1917-1932.
    • (2007) J. Proteome Res. , vol.6 , pp. 1917-1932
    • Xie, H.1    Vucetic, S.2    Iakoucheva, L.M.3    Oldfield, C.J.4    Dunker, A.K.5    Obradovic, Z.6    Uversky, V.N.7
  • 56
    • 70349335582 scopus 로고    scopus 로고
    • The S-phase checkpoint is required to respond to R-loops accumulated in THO mutants
    • Gomez-Gonzalez, B., Felipe-Abrio, I. and Aguilera, A. (2009) The S-phase checkpoint is required to respond to R-loops accumulated in THO mutants. Mol. Cell Biol., 29, 5203-5213.
    • (2009) Mol. Cell Biol. , vol.29 , pp. 5203-5213
    • Gomez-Gonzalez, B.1    Felipe-Abrio, I.2    Aguilera, A.3
  • 57
    • 77958169154 scopus 로고    scopus 로고
    • Genomic expression program involving the Haa1p-regulon in Saccharomyces cerevisiae response to acetic acid
    • Mira, N.P., Becker, J.D. and Sa-Correia, I. (2010) Genomic expression program involving the Haa1p-regulon in Saccharomyces cerevisiae response to acetic acid. OMICS, 14, 587-601.
    • (2010) OMICS , vol.14 , pp. 587-601
    • Mira, N.P.1    Becker, J.D.2    Sa-Correia, I.3
  • 58
    • 77958162502 scopus 로고    scopus 로고
    • Adaptive response and tolerance to weak acids in Saccharomyces cerevisiae: A genome-wide view
    • Mira, N.P., Teixeira, M.C. and Sa-Correia, I. (2010) Adaptive response and tolerance to weak acids in Saccharomyces cerevisiae: a genome-wide view. OMICS, 14, 525-540.
    • (2010) OMICS , vol.14 , pp. 525-540
    • Mira, N.P.1    Teixeira, M.C.2    Sa-Correia, I.3
  • 59
    • 0037086643 scopus 로고    scopus 로고
    • Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover
    • Hardeland, U., Steinacher, R., Jiricny, J. and Schar, P. (2002) Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover. EMBO J., 21, 1456-1464.
    • (2002) EMBO J. , vol.21 , pp. 1456-1464
    • Hardeland, U.1    Steinacher, R.2    Jiricny, J.3    Schar, P.4
  • 60
    • 1942422565 scopus 로고    scopus 로고
    • SUMO modification of heterogeneous nuclear ribonucleoproteins
    • Vassileva, M.T. and Matunis, M.J. (2004) SUMO modification of heterogeneous nuclear ribonucleoproteins. Mol. Cell Biol., 24, 3623-3632.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 3623-3632
    • Vassileva, M.T.1    Matunis, M.J.2
  • 62
    • 84869091913 scopus 로고    scopus 로고
    • Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair
    • Psakhye, I. and Jentsch, S. (2012) Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair. Cell, 151, 807-820.
    • (2012) Cell , vol.151 , pp. 807-820
    • Psakhye, I.1    Jentsch, S.2
  • 63
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: A history of modification
    • Hay, R.T. (2005) SUMO: a history of modification. Mol. Cell, 18, 1-12.
    • (2005) Mol. Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 64
    • 80054736893 scopus 로고    scopus 로고
    • An ataxia-telangiectasia-mutated (ATM) kinase mediated response to DNA damage down-regulates the mRNA-binding potential of THOC5
    • Ramachandran, S., Tran, D.D., Klebba-Faerber, S., Kardinal, C., Whetton, A.D. and Tamura, T. (2011) An ataxia-telangiectasia-mutated (ATM) kinase mediated response to DNA damage down-regulates the mRNA-binding potential of THOC5. RNA, 17, 1957-1966.
    • (2011) RNA , vol.17 , pp. 1957-1966
    • Ramachandran, S.1    Tran, D.D.2    Klebba-Faerber, S.3    Kardinal, C.4    Whetton, A.D.5    Tamura, T.6
  • 67
    • 58649121693 scopus 로고    scopus 로고
    • Cotranscriptional recruitment of the mRNA export factor Yra1 by direct interaction with the 3′-end processing factor Pcf11
    • Johnson, S.A., Cubberley, G. and Bentley, D.L. (2009) Cotranscriptional recruitment of the mRNA export factor Yra1 by direct interaction with the 3′-end processing factor Pcf11. Mol. Cell, 33, 215-226.
    • (2009) Mol. Cell , vol.33 , pp. 215-226
    • Johnson, S.A.1    Cubberley, G.2    Bentley, D.L.3
  • 68
    • 80054709866 scopus 로고    scopus 로고
    • Cotranscriptional association of mRNA export factor Yra1 with C-terminal domain of RNA polymerase II
    • MacKellar, A.L. and Greenleaf, A.L. (2011) Cotranscriptional association of mRNA export factor Yra1 with C-terminal domain of RNA polymerase II. J. Biol. Chem., 286, 36385-36395.
    • (2011) J. Biol. Chem. , vol.286 , pp. 36385-36395
    • MacKellar, A.L.1    Greenleaf, A.L.2
  • 69
    • 4444290337 scopus 로고    scopus 로고
    • Screening the yeast deletant mutant collection for hypersensitivity and hyper-resistance to sorbate, a weak organic acid food preservative
    • Mollapour, M., Fong, D., Balakrishnan, K., Harris, N., Thompson, S., Schuller, C., Kuchler, K. and Piper, P.W. (2004) Screening the yeast deletant mutant collection for hypersensitivity and hyper-resistance to sorbate, a weak organic acid food preservative. Yeast, 21, 927-946.
    • (2004) Yeast , vol.21 , pp. 927-946
    • Mollapour, M.1    Fong, D.2    Balakrishnan, K.3    Harris, N.4    Thompson, S.5    Schuller, C.6    Kuchler, K.7    Piper, P.W.8
  • 70
    • 33747337558 scopus 로고    scopus 로고
    • Yeast genes involved in response to lactic acid and acetic acid: Acidic conditions caused by the organic acids in Saccharomyces cerevisiae cultures induce expression of intracellular metal metabolism genes regulated by Aft1p
    • Kawahata, M., Masaki, K., Fujii, T. and Iefuji, H. (2006) Yeast genes involved in response to lactic acid and acetic acid: acidic conditions caused by the organic acids in Saccharomyces cerevisiae cultures induce expression of intracellular metal metabolism genes regulated by Aft1p. FEMS Yeast Res., 6, 924-936.
    • (2006) FEMS Yeast Res. , vol.6 , pp. 924-936
    • Kawahata, M.1    Masaki, K.2    Fujii, T.3    Iefuji, H.4
  • 71
    • 77958135565 scopus 로고    scopus 로고
    • Genome-wide identification of Saccharomyces cerevisiae genes required for tolerance to acetic acid
    • Mira, N.P., Palma, M., Guerreiro, J.F. and Sa-Correia, I. (2010) Genome-wide identification of Saccharomyces cerevisiae genes required for tolerance to acetic acid. Microb. Cell Fact., 9, 79.
    • (2010) Microb. Cell Fact. , vol.9 , pp. 79
    • Mira, N.P.1    Palma, M.2    Guerreiro, J.F.3    Sa-Correia, I.4
  • 72
    • 55549097135 scopus 로고    scopus 로고
    • Exonucleolysis is required for nuclear mRNA quality control in yeast THO mutants
    • Assenholt, J., Mouaikel, J., Andersen, K.R., Brodersen, D.E., Libri, D. and Jensen, T.H. (2008) Exonucleolysis is required for nuclear mRNA quality control in yeast THO mutants. RNA, 14, 2305-2313.
    • (2008) RNA , vol.14 , pp. 2305-2313
    • Assenholt, J.1    Mouaikel, J.2    Andersen, K.R.3    Brodersen, D.E.4    Libri, D.5    Jensen, T.H.6


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