메뉴 건너뛰기




Volumn 287, Issue 18, 2012, Pages 14772-14781

Yeast mitochondrial leucyl-tRNA synthetase CP1 domain has functionally diverged to accommodate RNA splicing at expense of hydrolytic editing

Author keywords

[No Author keywords available]

Indexed keywords

AMINOACYLATION; E. COLI; FULL-LENGTH ENZYMES; GROUP I INTRONS; IN-VITRO; PROTEIN SYNTHESIS; RNA SPLICING; SYNTHETASES;

EID: 84860379061     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.322412     Document Type: Article
Times cited : (17)

References (38)
  • 1
    • 0033198765 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases. A family of expanding functions
    • Martinis, S. A., Plateau, P., Cavarelli, J., and Florentz, C. (1999) Aminoacyl-tRNA synthetases. A family of expanding functions. EMBO J. 18, 4591-4596
    • (1999) EMBO J. , vol.18 , pp. 4591-4596
    • Martinis, S.A.1    Plateau, P.2    Cavarelli, J.3    Florentz, C.4
  • 2
    • 0025001288 scopus 로고
    • Involvement of aminoacyl-tRNA synthetases and other proteins in group I and group II intron splicing
    • Lambowitz, A. M., and Perlman, P. S. (1990) Involvement of aminoacyl-tRNA synthetases and other proteins in group I and group II intron splicing. Trends Biochem. Sci. 15, 440-444
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 440-444
    • Lambowitz, A.M.1    Perlman, P.S.2
  • 3
    • 0033782994 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis
    • Ibba, M., and Soll, D. (2000) Aminoacyl-tRNA synthesis. Annu. Rev. Biochem. 69, 617-650
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 617-650
    • Ibba, M.1    Soll, D.2
  • 4
    • 0023958916 scopus 로고
    • The NAM2 proteins from S. cerevisiae and S. douglasii are mitochondrial leucyl- tRNA synthetases and are involved in mRNA splicing
    • Herbert, C. J., Labouesse, M., Dujardin, G., and Slonimski, P. P. (1988) The NAM2 proteins from S. cerevisiae and S. douglasii are mitochondrial leucyl- tRNA synthetases and are involved in mRNA splicing. EMBO J. 7, 473-483
    • (1988) EMBO J. , vol.7 , pp. 473-483
    • Herbert, C.J.1    Labouesse, M.2    Dujardin, G.3    Slonimski, P.P.4
  • 5
    • 0025604577 scopus 로고
    • The yeast mitochondrial leucyl-tRNA synthetase is a splicing factor for the excision of several group I introns
    • Labouesse, M. (1990) The yeast mitochondrial leucyl-tRNA synthetase is a splicing factor for the excision of several group I introns. Mol. Gen. Genet. 224, 209-221
    • (1990) Mol. Gen. Genet. , vol.224 , pp. 209-221
    • Labouesse, M.1
  • 6
    • 0021887990 scopus 로고
    • The yeast nuclear gene NAM2 is essential for mitochondrial DNA integrity and can cure a mitochondrial RNA-maturase deficiency
    • Labouesse, M., Dujardin, G., and Slonimski, P. P. (1985) The yeast nuclear gene NAM2 is essential for mitochondrial DNA integrity and can cure a mitochondrial RNA-maturase deficiency. Cell 41, 133-143
    • (1985) Cell , vol.41 , pp. 133-143
    • Labouesse, M.1    Dujardin, G.2    Slonimski, P.P.3
  • 7
    • 0023669147 scopus 로고
    • A protein required for splicing group I introns in Neurospora mitochondria is mitochondrial tyrosyl-tRNA synthetase or a derivative thereof
    • Akins, R. A., and Lambowitz, A. M. (1987) A protein required for splicing group I introns in Neurospora mitochondria is mitochondrial tyrosyl-tRNA synthetase or a derivative thereof. Cell 50, 331-345
    • (1987) Cell , vol.50 , pp. 331-345
    • Akins, R.A.1    Lambowitz, A.M.2
  • 8
    • 43149110609 scopus 로고    scopus 로고
    • Identification and evolution of fungal mitochondrial tyrosyl-tRNA synthetases with group I intron splicing activity
    • Paukstelis, P. J., and Lambowitz, A. M. (2008) Identification and evolution of fungal mitochondrial tyrosyl-tRNA synthetases with group I intron splicing activity. Proc. Natl. Acad. Sci. U.S.A. 105, 6010-6015
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 6010-6015
    • Paukstelis, P.J.1    Lambowitz, A.M.2
  • 9
    • 0023303234 scopus 로고
    • Three suppressor mutations which cure a mitochondrial RNA maturase deficiency occur at the same codon in the open reading frame of the nuclear NAM2 gene
    • Labouesse, M., Herbert, C. J., Dujardin, G., and Slonimski, P. P. (1987) Three suppressor mutations which cure a mitochondrial RNA maturase deficiency occur at the same codon in the open reading frame of the nuclear NAM2 gene. EMBO J. 6, 713-721
    • (1987) EMBO J. , vol.6 , pp. 713-721
    • Labouesse, M.1    Herbert, C.J.2    Dujardin, G.3    Slonimski, P.P.4
  • 10
    • 0021503488 scopus 로고
    • Molecular basis of the "box effect." A maturase deficiency leading to the absence of splicing of two introns located in two split genes of yeast mitochondrial DNA
    • Labouesse, M., Netter, P., and Schroeder, R. (1984) Molecular basis of the "box effect." A maturase deficiency leading to the absence of splicing of two introns located in two split genes of yeast mitochondrial DNA. Eur. J. Biochem. 144, 85-93
    • (1984) Eur. J. Biochem. , vol.144 , pp. 85-93
    • Labouesse, M.1    Netter, P.2    Schroeder, R.3
  • 11
    • 0020318374 scopus 로고
    • Critical sequences within mitochondrial introns. Pleiotropic mRNA maturase and cis-dominant signals of the box intron controlling reductase and oxidase
    • De La Salle, H., Jacq, C., and Slonimski, P. P. (1982) Critical sequences within mitochondrial introns. Pleiotropic mRNA maturase and cis-dominant signals of the box intron controlling reductase and oxidase. Cell 28, 721-732
    • (1982) Cell , vol.28 , pp. 721-732
    • De La Salle, H.1    Jacq, C.2    Slonimski, P.P.3
  • 12
    • 11844297811 scopus 로고    scopus 로고
    • The splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function
    • Huang, H. R., Rowe, C. E., Mohr, S., Jiang, Y., Lambowitz, A. M., and Perlman, P. S. (2005) The splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function. Proc. Natl. Acad. Sci. U.S.A. 102, 163-168
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 163-168
    • Huang, H.R.1    Rowe, C.E.2    Mohr, S.3    Jiang, Y.4    Lambowitz, A.M.5    Perlman, P.S.6
  • 13
    • 0034566685 scopus 로고    scopus 로고
    • The bI4 group I intron binds directly to both its protein splicing partners, a tRNA synthetase and maturase, to facilitate RNA splicing activity
    • Rho, S. B., and Martinis, S. A. (2000) The bI4 group I intron binds directly to both its protein splicing partners, a tRNA synthetase and maturase, to facilitate RNA splicing activity. RNA 6, 1882-1894
    • (2000) RNA , vol.6 , pp. 1882-1894
    • Rho, S.B.1    Martinis, S.A.2
  • 14
    • 70350383756 scopus 로고    scopus 로고
    • Leucyl-tRNA synthetase-dependent and -independent activation of a group I intron
    • Boniecki, M. T., Rho, S. B., Tukalo, M., Hsu, J. L., Romero, E. P., and Martinis, S. A. (2009) Leucyl-tRNA synthetase-dependent and -independent activation of a group I intron. J. Biol. Chem. 284, 26243-26250
    • (2009) J. Biol. Chem. , vol.284 , pp. 26243-26250
    • Boniecki, M.T.1    Rho, S.B.2    Tukalo, M.3    Hsu, J.L.4    Romero, E.P.5    Martinis, S.A.6
  • 15
    • 0023202876 scopus 로고
    • Evidence for dispensable sequences inserted into a nucleotide fold
    • Starzyk, R. M., Webster, T. A., and Schimmel, P. (1987) Evidence for dispensable sequences inserted into a nucleotide fold. Science 237, 1614-1618
    • (1987) Science , vol.237 , pp. 1614-1618
    • Starzyk, R.M.1    Webster, T.A.2    Schimmel, P.3
  • 16
    • 0026087217 scopus 로고
    • Sequence determination and modeling of structural motifs for the smallest monomeric aminoacyl-tRNA synthetase
    • Hou, Y. M., Shiba, K., Mottes, C., and Schimmel, P. (1991) Sequence determination and modeling of structural motifs for the smallest monomeric aminoacyl-tRNA synthetase. Proc. Natl. Acad. Sci. U.S.A. 88, 976-980
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 976-980
    • Hou, Y.M.1    Shiba, K.2    Mottes, C.3    Schimmel, P.4
  • 17
    • 0037121930 scopus 로고    scopus 로고
    • An inserted region of leucyl-tRNA synthetase plays a critical role in group I intron splicing
    • Rho, S. B., Lincecum, T. L., Jr., and Martinis, S. A. (2002) An inserted region of leucyl-tRNA synthetase plays a critical role in group I intron splicing. EMBO J. 21, 6874-6881
    • (2002) EMBO J. , vol.21 , pp. 6874-6881
    • Rho, S.B.1    Lincecum Jr., T.L.2    Martinis, S.A.3
  • 18
    • 33747338033 scopus 로고    scopus 로고
    • Functional divergence of a unique C-terminal domain of leucyl-tRNA synthetase to accommodate its splicing and aminoacylation roles
    • Hsu, J. L., Rho, S. B., Vannella, K. M., and Martinis, S. A. (2006) Functional divergence of a unique C-terminal domain of leucyl-tRNA synthetase to accommodate its splicing and aminoacylation roles. J. Biol. Chem. 281, 23075-23082
    • (2006) J. Biol. Chem. , vol.281 , pp. 23075-23082
    • Hsu, J.L.1    Rho, S.B.2    Vannella, K.M.3    Martinis, S.A.4
  • 20
    • 0034657687 scopus 로고    scopus 로고
    • The 2 Å crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue
    • Cusack, S., Yaremchuk, A., and Tukalo, M. (2000) The 2 Å crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue. EMBO J. 19, 2351-2361
    • (2000) EMBO J. , vol.19 , pp. 2351-2361
    • Cusack, S.1    Yaremchuk, A.2    Tukalo, M.3
  • 21
    • 34249687080 scopus 로고    scopus 로고
    • Isolated CP1 domain of Escherichia coli leucyl-tRNA synthetase is dependent on flanking hinge motifs for amino acid editing activity
    • Betha, A. K., Williams, A. M., and Martinis, S. A. (2007) Isolated CP1 domain of Escherichia coli leucyl-tRNA synthetase is dependent on flanking hinge motifs for amino acid editing activity. Biochemistry 46, 6258-6267
    • (2007) Biochemistry , vol.46 , pp. 6258-6267
    • Betha, A.K.1    Williams, A.M.2    Martinis, S.A.3
  • 22
    • 58049211881 scopus 로고    scopus 로고
    • CP1- dependent partitioning of pretransfer and posttransfer editing in leucyl-tRNA synthetase
    • Boniecki, M. T., Vu, M. T., Betha, A. K., and Martinis, S. A. (2008) CP1- dependent partitioning of pretransfer and posttransfer editing in leucyl-tRNA synthetase. Proc. Natl. Acad. Sci. U.S.A. 105, 19223-19228
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 19223-19228
    • Boniecki, M.T.1    Vu, M.T.2    Betha, A.K.3    Martinis, S.A.4
  • 23
    • 0029910976 scopus 로고    scopus 로고
    • In vitro mutagenesis of the mitochondrial leucyl tRNA synthetase of Saccharomyces cerevisiae shows that the suppressor activity of the mutant proteins is related to the splicing function of the wild type protein
    • Li, G. Y., Bécam, A. M., Slonimski, P. P., and Herbert, C. J. (1996) In vitro mutagenesis of the mitochondrial leucyl tRNA synthetase of Saccharomyces cerevisiae shows that the suppressor activity of the mutant proteins is related to the splicing function of the wild type protein. Mol. Gen. Genet. 252, 667-675
    • (1996) Mol. Gen. Genet. , vol.252 , pp. 667-675
    • Li, G.Y.1    Bécam, A.M.2    Slonimski, P.P.3    Herbert, C.J.4
  • 24
    • 0023424907 scopus 로고
    • Construction of a yeast strain devoid of mitochondrial introns and its use to screen nuclear genes involved in mitochondrial splicing
    • Séraphin, B., Boulet, A., Simon, M., and Faye, G. (1987) Construction of a yeast strain devoid of mitochondrial introns and its use to screen nuclear genes involved in mitochondrial splicing. Proc. Natl. Acad. Sci. U.S.A. 84, 6810-6814
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 6810-6814
    • Séraphin, B.1    Boulet, A.2    Simon, M.3    Faye, G.4
  • 25
    • 33845944361 scopus 로고    scopus 로고
    • A viable amino acid editing activity in the leucyl-tRNA synthetase CP1- splicing domain is not required in the yeast mitochondria
    • Karkhanis, V. A., Boniecki, M. T., Poruri, K., and Martinis, S. A. (2006) A viable amino acid editing activity in the leucyl-tRNA synthetase CP1- splicing domain is not required in the yeast mitochondria. J. Biol. Chem. 281, 33217-33225
    • (2006) J. Biol. Chem. , vol.281 , pp. 33217-33225
    • Karkhanis, V.A.1    Boniecki, M.T.2    Poruri, K.3    Martinis, S.A.4
  • 26
    • 0034610278 scopus 로고    scopus 로고
    • A prokaryote and human tRNA synthetase provide an essential RNA splicing function in yeast mitochondria
    • Houman, F., Rho, S. B., Zhang, J., Shen, X., Wang, C. C., Schimmel, P., and Martinis, S. A. (2000) A prokaryote and human tRNA synthetase provide an essential RNA splicing function in yeast mitochondria. Proc. Natl. Acad. Sci. U.S.A. 97, 13743-13748
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13743-13748
    • Houman, F.1    Rho, S.B.2    Zhang, J.3    Shen, X.4    Wang, C.C.5    Schimmel, P.6    Martinis, S.A.7
  • 27
    • 0023953676 scopus 로고
    • Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro
    • Sampson, J. R., and Uhlenbeck, O. C. (1988) Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro. Proc. Natl. Acad. Sci. U.S.A. 85, 1033-1037
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 1033-1037
    • Sampson, J.R.1    Uhlenbeck, O.C.2
  • 28
    • 0023840230 scopus 로고
    • ompT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification
    • Grodberg, J., and Dunn, J. J. (1988) ompT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification. J. Bacteriol. 170, 1245-1253
    • (1988) J. Bacteriol. , vol.170 , pp. 1245-1253
    • Grodberg, J.1    Dunn, J.J.2
  • 29
    • 0015522966 scopus 로고
    • Transfer ribonucleic acid synthetase catalyzed deacylation of aminoacyl transfer ribonucleic acid in the absence of adenosine monophosphate and pyrophosphate
    • Schreier, A. A., and Schimmel, P. R. (1972) Transfer ribonucleic acid synthetase catalyzed deacylation of aminoacyl transfer ribonucleic acid in the absence of adenosine monophosphate and pyrophosphate. Biochemistry 11, 1582-1589
    • (1972) Biochemistry , vol.11 , pp. 1582-1589
    • Schreier, A.A.1    Schimmel, P.R.2
  • 30
    • 33847132709 scopus 로고    scopus 로고
    • Molecular and functional dissection of a putative RNA binding region in yeast mitochondrial leucyl-tRNA synthetase
    • Nawaz, M. H., Pang, Y. L., and Martinis, S. A. (2007) Molecular and functional dissection of a putative RNA binding region in yeast mitochondrial leucyl-tRNA synthetase. J. Mol. Biol. 367, 384-394
    • (2007) J. Mol. Biol. , vol.367 , pp. 384-394
    • Nawaz, M.H.1    Pang, Y.L.2    Martinis, S.A.3
  • 31
    • 42349092094 scopus 로고    scopus 로고
    • Functional segregation of a predicted "hinge" site within the β-strand linkers of Escherichia coli leucyl- tRNA synthetase
    • Mascarenhas, A. P., and Martinis, S. A. (2008) Functional segregation of a predicted "hinge" site within the β-strand linkers of Escherichia coli leucyl- tRNA synthetase. Biochemistry 47, 4808-4816
    • (2008) Biochemistry , vol.47 , pp. 4808-4816
    • Mascarenhas, A.P.1    Martinis, S.A.2
  • 33
    • 27144477810 scopus 로고    scopus 로고
    • The crystal structure of leucyl-tRNA synthetase complexed with tRNALeu in the post-transfer-editing conformation
    • Tukalo, M., Yaremchuk, A., Fukunaga, R., Yokoyama, S., and Cusack, S. (2005) The crystal structure of leucyl-tRNA synthetase complexed with tRNALeu in the post-transfer-editing conformation. Nat. Struct. Mol. Biol. 12, 923-930
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 923-930
    • Tukalo, M.1    Yaremchuk, A.2    Fukunaga, R.3    Yokoyama, S.4    Cusack, S.5
  • 34
    • 0024989581 scopus 로고
    • Function of Neurospora mitochondrial tyrosyl-tRNA synthetase in RNA splicing requires an idiosyncratic domain not found in other synthetases
    • Cherniack, A. D., Garriga, G., Kittle, J. D., Jr., Akins, R. A., and Lambowitz, A. M. (1990) Function of Neurospora mitochondrial tyrosyl-tRNA synthetase in RNA splicing requires an idiosyncratic domain not found in other synthetases. Cell 62, 745-755
    • (1990) Cell , vol.62 , pp. 745-755
    • Cherniack, A.D.1    Garriga, G.2    Kittle Jr., J.D.3    Akins, R.A.4    Lambowitz, A.M.5
  • 35
    • 38049086319 scopus 로고    scopus 로고
    • Structure of a tyrosyl-tRNA synthetase splicing factor bound to a group I intron RNA
    • Paukstelis, P. J., Chen, J. H., Chase, E., Lambowitz, A. M., and Golden, B. L. (2008) Structure of a tyrosyl-tRNA synthetase splicing factor bound to a group I intron RNA. Nature 451, 94-97
    • (2008) Nature , vol.451 , pp. 94-97
    • Paukstelis, P.J.1    Chen, J.H.2    Chase, E.3    Lambowitz, A.M.4    Golden, B.L.5
  • 36
    • 27144520077 scopus 로고    scopus 로고
    • Aminoacylation complex structures of leucyl-tRNA synthetase and tRNALeu reveal two modes of discriminator- base recognition
    • Fukunaga, R., and Yokoyama, S. (2005) Aminoacylation complex structures of leucyl-tRNA synthetase and tRNALeu reveal two modes of discriminator- base recognition. Nat. Struct. Mol. Biol. 12, 915-922
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 915-922
    • Fukunaga, R.1    Yokoyama, S.2
  • 37
    • 33644858728 scopus 로고    scopus 로고
    • Mutational unmasking of a tRNA-dependent pathway for preventing genetic code ambiguity
    • Williams, A. M., and Martinis, S. A. (2006) Mutational unmasking of a tRNA-dependent pathway for preventing genetic code ambiguity. Proc. Natl. Acad. Sci. U.S.A. 103, 3586-3591
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 3586-3591
    • Williams, A.M.1    Martinis, S.A.2
  • 38
    • 0032858475 scopus 로고    scopus 로고
    • The peptide bond between Glu-292-Ala-293 of Escherichia coli leucyl-tRNA synthetase is essential for its activity
    • Li, T., Guo, N., Xia, X., Wang, E. D., and Wang, Y. L. (1999) The peptide bond between Glu-292-Ala-293 of Escherichia coli leucyl-tRNA synthetase is essential for its activity. Biochemistry 38, 13063-13069
    • (1999) Biochemistry , vol.38 , pp. 13063-13069
    • Li, T.1    Guo, N.2    Xia, X.3    Wang, E.D.4    Wang, Y.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.