메뉴 건너뛰기




Volumn 288, Issue 38, 2013, Pages 27415-27422

Partitioning of the nuclear and mitochondrial tRNa 3'-end processing activities between two different proteins in Schizosaccharomyces pombe

Author keywords

[No Author keywords available]

Indexed keywords

CAENORHABDITIS ELEGANS; DIFFERENTIAL EXPRESSIONS; DROSOPHILA MELANOGASTER; FISSION YEAST; PROCESSING ACTIVITY; PROTEIN LEVEL; SCHIZOSACCHAROMYCES POMBE; TEMPERATURE-SENSITIVE;

EID: 84884553893     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.501569     Document Type: Article
Times cited : (12)

References (48)
  • 1
    • 72849106592 scopus 로고    scopus 로고
    • RNA processing and its regulation: Global insights into biological networks
    • Licatalosi, D. D., and Darnell, R. B. (2010) RNA processing and its regulation: global insights into biological networks. Nat. Rev. Genet. 11, 75-87
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 75-87
    • Licatalosi, D.D.1    Darnell, R.B.2
  • 3
    • 77956276464 scopus 로고    scopus 로고
    • TRNA biology charges to the front
    • Phizicky, E. M., and Hopper, A. K. (2010) tRNA biology charges to the front. Genes Dev. 24, 1832-1860
    • (2010) Genes Dev. , vol.24 , pp. 1832-1860
    • Phizicky, E.M.1    Hopper, A.K.2
  • 4
    • 84864318790 scopus 로고    scopus 로고
    • Of P and Z: Mitochondrial tRNA processing enzymes
    • Rossmanith, W. (2012) Of P and Z: mitochondrial tRNA processing enzymes. Biochim. Biophys. Acta 1819, 1017-1026
    • (2012) Biochim. Biophys. Acta , vol.1819 , pp. 1017-1026
    • Rossmanith, W.1
  • 5
    • 33745815336 scopus 로고    scopus 로고
    • Separate RNA-binding surfaces on the multifunctional La protein mediate distinguishable activities in tRNA maturation
    • Huang, Y., Bayfield, M. A., Intine, R. V., and Maraia, R. J. (2006) Separate RNA-binding surfaces on the multifunctional La protein mediate distinguishable activities in tRNA maturation. Nat. Struct. Mol. Biol. 13, 611-618
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 611-618
    • Huang, Y.1    Bayfield, M.A.2    Intine, R.V.3    Maraia, R.J.4
  • 6
    • 0030904723 scopus 로고    scopus 로고
    • The yeast La protein is required for the 3'-endonucleolytic cleavage that matures tRNA precursors
    • Yoo, C. J., and Wolin, S. L. (1997) The yeast La protein is required for the 3'-endonucleolytic cleavage that matures tRNA precursors. Cell 89, 393-402
    • (1997) Cell , vol.89 , pp. 393-402
    • Yoo, C.J.1    Wolin, S.L.2
  • 7
    • 44149101017 scopus 로고    scopus 로고
    • Competition between the Rex1 exonuclease and the La protein affects both Trf4p-mediated RNA quality control and pre-tRNA maturation
    • Copela, L. A., Fernandez, C. F., Sherrer, R. L., and Wolin, S. L. (2008) Competition between the Rex1 exonuclease and the La protein affects both Trf4p-mediated RNA quality control and pre-tRNA maturation. RNA 14, 1214-1227
    • (2008) RNA , vol.14 , pp. 1214-1227
    • Copela, L.A.1    Fernandez, C.F.2    Sherrer, R.L.3    Wolin, S.L.4
  • 8
    • 58549100937 scopus 로고    scopus 로고
    • Rex1p deficiency leads to accumulation of precursor initiator tRNAMet and polyadenylation of substrate RNAs in Saccharomyces cerevisiae
    • Ozanick, S. G., Wang, X., Costanzo, M., Brost, R. L., Boone, C., and Anderson, J. T. (2009) Rex1p deficiency leads to accumulation of precursor initiator tRNAMet and polyadenylation of substrate RNAs in Saccharomyces cerevisiae. Nucleic Acids Res. 37, 298-308
    • (2009) Nucleic Acids Res. , vol.37 , pp. 298-308
    • Ozanick, S.G.1    Wang, X.2    Costanzo, M.3    Brost, R.L.4    Boone, C.5    Anderson, J.T.6
  • 9
    • 0037439213 scopus 로고    scopus 로고
    • TRNA transfers to the limelight
    • Hopper, A. K., and Phizicky, E. M. (2003) tRNA transfers to the limelight. Genes Dev. 17, 162-180
    • (2003) Genes Dev. , vol.17 , pp. 162-180
    • Hopper, A.K.1    Phizicky, E.M.2
  • 10
    • 33847792061 scopus 로고    scopus 로고
    • Mitochondrial transcription and its regulation in mammalian cells
    • Asin-Cayuela, J., and Gustafsson, C. M. (2007) Mitochondrial transcription and its regulation in mammalian cells. Trends Biochem. Sci. 32, 111-117
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 111-117
    • Asin-Cayuela, J.1    Gustafsson, C.M.2
  • 11
    • 42049114034 scopus 로고    scopus 로고
    • Transcriptional paradigms in mammalian mitochondrial biogenesis and function
    • Scarpulla, R. C. (2008) Transcriptional paradigms in mammalian mitochondrial biogenesis and function. Physiol. Rev. 88, 611-638
    • (2008) Physiol. Rev. , vol.88 , pp. 611-638
    • Scarpulla, R.C.1
  • 12
    • 0032496669 scopus 로고    scopus 로고
    • Usage of non-canonical promoter sequence by the yeast mitochondrial RNA polymerase
    • Biswas, T. K. (1998) Usage of non-canonical promoter sequence by the yeast mitochondrial RNA polymerase. Gene 212, 305-314
    • (1998) Gene , vol.212 , pp. 305-314
    • Biswas, T.K.1
  • 13
    • 0025695227 scopus 로고
    • Control of mitochondrial gene expression in Saccharomyces cerevisiae
    • Costanzo, M. C., and Fox, T. D. (1990) Control of mitochondrial gene expression in Saccharomyces cerevisiae. Annu. Rev. Genet. 24, 91-113
    • (1990) Annu. Rev. Genet. , vol.24 , pp. 91-113
    • Costanzo, M.C.1    Fox, T.D.2
  • 14
    • 0028206309 scopus 로고
    • Regulation of mitochondrial gene expression in Saccharomyces cerevisiae
    • Dieckmann, C. L., and Staples, R. R. (1994) Regulation of mitochondrial gene expression in Saccharomyces cerevisiae. Int. Rev. Cytol. 152, 145-181
    • (1994) Int. Rev. Cytol. , vol.152 , pp. 145-181
    • Dieckmann, C.L.1    Staples, R.R.2
  • 15
    • 79960251405 scopus 로고    scopus 로고
    • Identification and characterization of the mitochondrial RNA polymerase and transcription factor in the fission yeast Schizosaccharomyces pombe
    • Jiang, H., Sun, W., Wang, Z., Zhang, J., Chen, D., and Murchie, A. I. (2011) Identification and characterization of the mitochondrial RNA polymerase and transcription factor in the fission yeast Schizosaccharomyces pombe. Nucleic Acids Res. 39, 5119-5130
    • (2011) Nucleic Acids Res. , vol.39 , pp. 5119-5130
    • Jiang, H.1    Sun, W.2    Wang, Z.3    Zhang, J.4    Chen, D.5    Murchie, A.I.6
  • 16
    • 17844366081 scopus 로고    scopus 로고
    • Transcription and RNAprocessing in fission yeast mitochondria
    • Schäfer, B., Hansen, M., and Lang, B. F. (2005) Transcription and RNAprocessing in fission yeast mitochondria. RNA 11, 785-795
    • (2005) RNA , vol.11 , pp. 785-795
    • Schäfer, B.1    Hansen, M.2    Lang, B.F.3
  • 17
    • 0019444843 scopus 로고
    • TRNA punctuation model of RNA processing in human mitochondria
    • Ojala, D., Montoya, J., and Attardi, G. (1981) tRNA punctuation model of RNA processing in human mitochondria. Nature 290, 470-474
    • (1981) Nature , vol.290 , pp. 470-474
    • Ojala, D.1    Montoya, J.2    Attardi, G.3
  • 18
    • 0022555846 scopus 로고
    • Genetics of mitochondrial biogenesis
    • Tzagoloff, A., and Myers, A. M. (1986) Genetics of mitochondrial biogenesis. Annu. Rev. Biochem. 55, 249-285
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 249-285
    • Tzagoloff, A.1    Myers, A.M.2
  • 19
    • 23644440813 scopus 로고    scopus 로고
    • RNA maturation in mitochondria of S
    • Schäfer, B. (2005) RNA maturation in mitochondria of S. cerevisiae and S. pombe. Gene 354, 80-85
    • (2005) Cerevisiae and S. Pombe. Gene , vol.354 , pp. 80-85
    • Schäfer, B.1
  • 20
    • 42949101518 scopus 로고    scopus 로고
    • Pet127 governs a 5'→3'-exonuclease important in maturation of apocytochrome b mRNA in Saccharomyces cerevisiae
    • Fekete, Z., Ellis, T. P., Schonauer, M. S., and Dieckmann, C. L. (2008) Pet127 governs a 5'→3'-exonuclease important in maturation of apocytochrome b mRNA in Saccharomyces cerevisiae. J. Biol. Chem. 283, 3767-3772
    • (2008) J. Biol. Chem. , vol.283 , pp. 3767-3772
    • Fekete, Z.1    Ellis, T.P.2    Schonauer, M.S.3    Dieckmann, C.L.4
  • 23
    • 33947360611 scopus 로고    scopus 로고
    • When all's zed and done: The structure and function of RNase Z in prokaryotes
    • Redko, Y., Li De La Sierra-Gallay, I., and Condon, C. (2007) When all's zed and done: the structure and function of RNase Z in prokaryotes. Nat. Rev. Microbiol. 5, 278-286
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 278-286
    • Redko, Y.1    Li De La Sierra-Gallay, I.2    Condon, C.3
  • 25
    • 34247157802 scopus 로고    scopus 로고
    • Nucleases of the metallo-'-lactamase family and their role in DNA and RNA metabolism
    • Dominski, Z. (2007) Nucleases of the metallo-'-lactamase family and their role in DNA and RNA metabolism. Crit. Rev. Biochem. Mol. Biol. 42, 67-93
    • (2007) Crit. Rev. Biochem. Mol. Biol. , vol.42 , pp. 67-93
    • Dominski, Z.1
  • 27
    • 77956468959 scopus 로고    scopus 로고
    • Identification and analysis of candidate fungal tRNA 3'-end processing endonucleases tRNase Zs, homologs of the putative prostate cancer susceptibility protein ELAC2. BMC Evol
    • Zhao, W., Yu, H., Li, S., and Huang, Y. (2010) Identification and analysis of candidate fungal tRNA 3'-end processing endonucleases tRNase Zs, homologs of the putative prostate cancer susceptibility protein ELAC2. BMC Evol. Biol. 10, 272
    • (2010) Biol. , vol.10 , pp. 272
    • Zhao, W.1    Yu, H.2    Li, S.3    Huang, Y.4
  • 28
    • 79960563960 scopus 로고    scopus 로고
    • A survey of green plant tRNA 3'-end processing enzyme tRNase Zs, homologs of the candidate prostate cancer susceptibility protein ELAC2
    • Fan, L., Wang, Z., Liu, J., Guo, W., Yan, J., and Huang, Y. (2011) A survey of green plant tRNA 3'-end processing enzyme tRNase Zs, homologs of the candidate prostate cancer susceptibility protein ELAC2. BMC Evol. Biol. 11, 219
    • (2011) BMC Evol. Biol. , vol.11 , pp. 219
    • Fan, L.1    Wang, Z.2    Liu, J.3    Guo, W.4    Yan, J.5    Huang, Y.6
  • 29
    • 69949152972 scopus 로고    scopus 로고
    • A fungal phylogeny based on 82 complete genomes using the composition vector method
    • Wang, H., Xu, Z., Gao, L., and Hao, B. (2009) A fungal phylogeny based on 82 complete genomes using the composition vector method. BMC Evol. Biol. 9, 195
    • (2009) BMC Evol. Biol. , vol.9 , pp. 195
    • Wang, H.1    Xu, Z.2    Gao, L.3    Hao, B.4
  • 30
    • 85046980054 scopus 로고    scopus 로고
    • Involvement of human ELAC2 gene product in 3'-end processing of mitochondrial tRNAs
    • Brzezniak, L. K., Bijata, M., Szczesny, R. J., and Stepien, P. P. (2011) Involvement of human ELAC2 gene product in 3'-end processing of mitochondrial tRNAs. RNA Biol. 8, 616-626
    • (2011) RNA Biol. , vol.8 , pp. 616-626
    • Brzezniak, L.K.1    Bijata, M.2    Szczesny, R.J.3    Stepien, P.P.4
  • 31
    • 79955716664 scopus 로고    scopus 로고
    • Localization of human RNase Z isoforms: Dual nuclear/mitochondrial targeting of the ELAC2 gene product by alternative translation initiation
    • Rossmanith, W. (2011) Localization of human RNase Z isoforms: dual nuclear/mitochondrial targeting of the ELAC2 gene product by alternative translation initiation. PLoS ONE 6, e19152
    • (2011) PLoS ONE , vol.6
    • Rossmanith, W.1
  • 33
    • 46749129676 scopus 로고    scopus 로고
    • Regulation of the human tRNase ZS gene expression
    • Takahashi, M., Takaku, H., and Nashimoto, M. (2008) Regulation of the human tRNase ZS gene expression. FEBS Lett. 582, 2532-2536
    • (2008) FEBS Lett. , vol.582 , pp. 2532-2536
    • Takahashi, M.1    Takaku, H.2    Nashimoto, M.3
  • 35
    • 84866014716 scopus 로고    scopus 로고
    • Identification and sequence analysis of metazoan tRNA 3'-end processing enzymes tRNase Zs
    • Wang, Z., Zheng, J., Zhang, X., Peng, J., Liu, J., and Huang, Y. (2012) Identification and sequence analysis of metazoan tRNA 3'-end processing enzymes tRNase Zs. PLoS ONE 7, e44264
    • (2012) PLoS ONE , vol.7
    • Wang, Z.1    Zheng, J.2    Zhang, X.3    Peng, J.4    Liu, J.5    Huang, Y.6
  • 36
    • 79951508787 scopus 로고    scopus 로고
    • RNAi knockdown of dRNaseZ, the Drosophila homolog of ELAC2, impairs growth of mitotic and endoreplicating tissues
    • Xie, X., Dubrovskaya, V. A., and Dubrovsky, E. B. (2011) RNAi knockdown of dRNaseZ, the Drosophila homolog of ELAC2, impairs growth of mitotic and endoreplicating tissues. Insect Biochem. Mol. Biol. 41, 167-177
    • (2011) Insect Biochem. Mol. Biol. , vol.41 , pp. 167-177
    • Xie, X.1    Dubrovskaya, V.A.2    Dubrovsky, E.B.3
  • 37
    • 4243087008 scopus 로고    scopus 로고
    • The N-terminal half-domain of the long form of tRNase Z is required for the RNase 65 activity
    • Takaku, H., Minagawa, A., Takagi, M., and Nashimoto, M. (2004) The N-terminal half-domain of the long form of tRNase Z is required for the RNase 65 activity. Nucleic Acids Res. 32, 4429-4438
    • (2004) Nucleic Acids Res. , vol.32 , pp. 4429-4438
    • Takaku, H.1    Minagawa, A.2    Takagi, M.3    Nashimoto, M.4
  • 38
    • 79952852361 scopus 로고    scopus 로고
    • The fission yeast Schizosaccharomyces pombe has two distinct tRNase ZLs encoded by two different genes and differentially targeted to the nucleus and mitochondria
    • Gan, X., Yang, J., Li, J., Yu, H., Dai, H., Liu, J., and Huang, Y. (2011) The fission yeast Schizosaccharomyces pombe has two distinct tRNase ZLs encoded by two different genes and differentially targeted to the nucleus and mitochondria. Biochem. J. 435, 103-111
    • (2011) Biochem. J. , vol.435 , pp. 103-111
    • Gan, X.1    Yang, J.2    Li, J.3    Yu, H.4    Dai, H.5    Liu, J.6    Huang, Y.7
  • 39
    • 70249111171 scopus 로고    scopus 로고
    • Functional conservation of tRNase ZL among Saccharomyces cerevisiae, Schizosaccharomyces pombe and humans
    • Zhao, Z., Su, W., Yuan, S., and Huang, Y. (2009) Functional conservation of tRNase ZL among Saccharomyces cerevisiae, Schizosaccharomyces pombe and humans. Biochem. J. 422, 483-492
    • (2009) Biochem. J. , vol.422 , pp. 483-492
    • Zhao, Z.1    Su, W.2    Yuan, S.3    Huang, Y.4
  • 41
    • 0026025891 scopus 로고
    • Molecular genetic analysis of fission yeast Schizosaccharomyces pombe
    • Moreno, S., Klar, A., and Nurse, P. (1991) Molecular genetic analysis of fission yeast Schizosaccharomyces pombe. Methods Enzymol. 194, 795-823
    • (1991) Methods Enzymol. , vol.194 , pp. 795-823
    • Moreno, S.1    Klar, A.2    Nurse, P.3
  • 42
    • 11844249959 scopus 로고    scopus 로고
    • Mutations in the RNA polymerase III subunit Rpc11p that decrease RNA 3' cleavage activity increase 3'-terminal oligo (U) length and La-dependent tRNA processing
    • Huang, Y., Intine, R. V., Mozlin, A., Hasson, S., and Maraia, R. J. (2005) Mutations in the RNA polymerase III subunit Rpc11p that decrease RNA 3' cleavage activity increase 3'-terminal oligo (U) length and La-dependent tRNA processing. Mol. Cell. Biol. 25, 621-636
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 621-636
    • Huang, Y.1    Intine, R.V.2    Mozlin, A.3    Hasson, S.4    Maraia, R.J.5
  • 43
    • 0036281765 scopus 로고    scopus 로고
    • Aberrant nuclear trafficking of La protein leads to disordered processing of associated precursor tRNAs
    • Intine, R. V., Dundr, M., Misteli, T., and Maraia, R. J. (2002) Aberrant nuclear trafficking of La protein leads to disordered processing of associated precursor tRNAs. Mol. Cell 9, 1113-1123
    • (2002) Mol. Cell , vol.9 , pp. 1113-1123
    • Intine, R.V.1    Dundr, M.2    Misteli, T.3    Maraia, R.J.4
  • 45
    • 0031469506 scopus 로고    scopus 로고
    • The La protein in Schizosaccharomyces pombe: A conserved yet dispensable phosphoprotein that functions in tRNA maturation
    • Van Horn, D. J., Yoo, C. J., Xue, D., Shi, H., and Wolin, S. L. (1997) The La protein in Schizosaccharomyces pombe: a conserved yet dispensable phosphoprotein that functions in tRNA maturation. RNA 3, 1434-1443
    • (1997) RNA , vol.3 , pp. 1434-1443
    • Van Horn, D.J.1    Yoo, C.J.2    Xue, D.3    Shi, H.4    Wolin, S.L.5
  • 46
    • 0027441494 scopus 로고
    • TATA box mutations in the Schizosaccharomyces pombe nmt1 promoter affect transcription efficiency but not the transcription start point or thiamine repressibility
    • Basi, G., Schmid, E., and Maundrell, K. (1993) TATA box mutations in the Schizosaccharomyces pombe nmt1 promoter affect transcription efficiency but not the transcription start point or thiamine repressibility. Gene 123, 131-136
    • (1993) Gene , vol.123 , pp. 131-136
    • Basi, G.1    Schmid, E.2    Maundrell, K.3
  • 47
    • 0346461447 scopus 로고    scopus 로고
    • The Caenorhabditis elegans homolog of the putative prostate cancer susceptibility gene ELAC2, hoe-1, plays a role in germline proliferation
    • Smith, M. M., and Levitan, D. J. (2004) The Caenorhabditis elegans homolog of the putative prostate cancer susceptibility gene ELAC2, hoe-1, plays a role in germline proliferation. Dev. Biol. 266, 151-160
    • (2004) Dev. Biol. , vol.266 , pp. 151-160
    • Smith, M.M.1    Levitan, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.