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Volumn 79, Issue 12, 1997, Pages 731-740

Cysteinyl-tRNA synthetase from Saccharomyces cerevisiae. Purification, characterization and assignment to the genomic sequence YNL247w

Author keywords

Cysteinyl tRNA synthetase; Genomic sequence YNL247w; Saccharomyces cerevisiae

Indexed keywords

CYSTEINE TRANSFER RNA; CYSTEINYL TRANSFER RIBONUCLEIC ACID SYNTHETASE; FUNGAL PROTEIN; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 0031404731     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(97)86931-3     Document Type: Article
Times cited : (11)

References (38)
  • 1
    • 0023061339 scopus 로고
    • Aminoacyl-tKNA synthetases; general scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs
    • Schimmel P (1987) Aminoacyl-tKNA synthetases; general scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs. Annu Rev Biochem 56, 125-158
    • (1987) Annu Rev Biochem , vol.56 , pp. 125-158
    • Schimmel, P.1
  • 2
    • 0027255483 scopus 로고
    • Cognition, medianism, and evolutionary relationships in aminoacyl-transfer RNA synthetases
    • Carter CW (1993) Cognition, medianism, and evolutionary relationships in aminoacyl-transfer RNA synthetases. Annu Rev Biochem 62, 715-748
    • (1993) Annu Rev Biochem , vol.62 , pp. 715-748
    • Carter, C.W.1
  • 3
    • 0025158208 scopus 로고
    • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
    • Eriani G, Delarue M, Poch O, Gangloff J. Moras D (1990) Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347, 203-206
    • (1990) Nature , vol.347 , pp. 203-206
    • Eriani, G.1    Delarue, M.2    Poch, O.3    Gangloff, J.4    Moras, D.5
  • 4
    • 0024392753 scopus 로고
    • Structure of E coli glutaminyl-tRNA synthetase complexed with tRNAGln and ATP at 2.8 angstrom resolution
    • Rould MA, Perona JJ, Söll D, Steitz ZA (1989) Structure of E coli glutaminyl-tRNA synthetase complexed with tRNAGln and ATP at 2.8 Angstrom resolution. Science 246, 1135-1142
    • (1989) Science , vol.246 , pp. 1135-1142
    • Rould, M.A.1    Perona, J.J.2    Söll, D.3    Steitz, Z.A.4
  • 5
    • 0025043116 scopus 로고
    • A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase
    • Cusack S, Berthet-Colominas C, Hartlein M, Nassar N, Leberman R (1990) A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase. Nature 347, 249-255
    • (1990) Nature , vol.347 , pp. 249-255
    • Cusack, S.1    Berthet-Colominas, C.2    Hartlein, M.3    Nassar, N.4    Leberman, R.5
  • 6
    • 0029099218 scopus 로고
    • Eleven down and nine to go
    • Cusack S (1995) Eleven down and nine to go. Nature Struct Biology 2, 824-831
    • (1995) Nature Struct Biology , vol.2 , pp. 824-831
    • Cusack, S.1
  • 7
    • 0030962189 scopus 로고    scopus 로고
    • Structural and functional considerations of the aminoacylation reaction
    • Arnez JG, Moras D (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22, 211-216
    • (1997) Trends Biochem Sci , vol.22 , pp. 211-216
    • Arnez, J.G.1    Moras, D.2
  • 8
    • 0025930249 scopus 로고
    • Aminoacyl-lRNA synthetase family from prokaryotes and eukaryotes; structural domains and their implications
    • Mirande M (1991) Aminoacyl-lRNA synthetase family from prokaryotes and eukaryotes; Structural domains and their implications. Prog Nucleic Acid Res Mol Biol 40, 95-142
    • (1991) Prog Nucleic Acid Res Mol Biol , vol.40 , pp. 95-142
    • Mirande, M.1
  • 9
    • 0031589946 scopus 로고    scopus 로고
    • The yeast genome directory
    • Goffeau A et al (1997) The yeast genome directory. Nature 387, 5-105
    • (1997) Nature , vol.387 , pp. 5-105
    • Goffeau, A.1
  • 10
    • 0031589946 scopus 로고    scopus 로고
    • The yeast genome directory
    • Gazetteer section
    • Goffeau A et al (1997) The yeast genome directory. Nature 387, Gazetteer section, 49
    • (1997) Nature , vol.387 , pp. 49
    • Goffeau, A.1
  • 11
    • 0014690584 scopus 로고
    • Purification and properties of the Lcysteinyl ribonucleic acid synthetase of baker's yeast
    • James HL, Bucovaz ET (1969) Purification and properties of the Lcysteinyl ribonucleic acid synthetase of baker's yeast. J Biol Chem 244, 3210-3216
    • (1969) J Biol Chem , vol.244 , pp. 3210-3216
    • James, H.L.1    Bucovaz, E.T.2
  • 12
    • 0018523162 scopus 로고
    • Macromolecular complexes of aminoacyl-tRNA synthetases from cukaryotes. 1. Extensive purification and characterization of the high-molecular-weight complex (es) of seven aminoacyl-tRNA synthetases from sheep liver
    • Kellermann O, Brevet A, Tonetti H, Waller JP (1979) Macromolecular complexes of aminoacyl-tRNA synthetases from cukaryotes. 1. Extensive purification and characterization of the high-molecular-weight complex (es) of seven aminoacyl-tRNA synthetases from sheep liver. Eur J Biochem 99, 541-550
    • (1979) Eur J Biochem , vol.99 , pp. 541-550
    • Kellermann, O.1    Brevet, A.2    Tonetti, H.3    Waller, J.P.4
  • 13
    • 0025776722 scopus 로고
    • Nucleotide and deduced amino acid sequence of human threonyl-tRNA synthetase reveals extensive homolocy to the Escherichia coli and yeast enzymes
    • Cruzen ME, Arfin SM (1991) Nucleotide and deduced amino acid sequence of human threonyl-tRNA synthetase reveals extensive homolocy to the Escherichia coli and yeast enzymes. J Biol Chem 266, 9919-9923
    • (1991) J Biol Chem , vol.266 , pp. 9919-9923
    • Cruzen, M.E.1    Arfin, S.M.2
  • 14
    • 0019334764 scopus 로고
    • Purification and structural characterization of rat liver thieonyl transfer ribonucleic acid synthetase
    • Dignam JD, Rhodes DG, Deutscher MP (1980) Purification and structural characterization of rat liver thieonyl transfer ribonucleic acid synthetase. Biochemistry 19, 4978-4984
    • (1980) Biochemistry , vol.19 , pp. 4978-4984
    • Dignam, J.D.1    Rhodes, D.G.2    Deutscher, M.P.3
  • 15
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0014817347 scopus 로고
    • Use of dimethyl suberimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins
    • Davies GE, Stark GR (1970) Use of dimethyl suberimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins. Proc Natl Acad Sci USA 66, 651-656
    • (1970) Proc Natl Acad Sci USA , vol.66 , pp. 651-656
    • Davies, G.E.1    Stark, G.R.2
  • 18
    • 0021877350 scopus 로고
    • Multiple forms of arginyl-and lysyl-tRNA synhetases in rat liver; a re-evaluation
    • Cirakoglu B, Waller J-P (1985) Multiple forms of arginyl-and lysyl-tRNA synhetases in rat liver; a re-evaluation. Biochim Biophys Acta 829, 173-179
    • (1985) Biochim Biophys Acta , vol.829 , pp. 173-179
    • Cirakoglu, B.1    Waller, J.-P.2
  • 21
    • 0020637308 scopus 로고
    • India ink staining of proteins on nitrocellulose paper
    • Hancock K. Tsang VCW (1983) India ink staining of proteins on nitrocellulose paper. Anal Biochem 133, 157-162
    • (1983) Anal Biochem , vol.133 , pp. 157-162
    • Hancock, K.1    Tsang, V.C.W.2
  • 22
    • 0017121494 scopus 로고
    • Arginyl-tRNA synthetase from baker's yeast. Purification and some properties
    • Gangloff J, Schutz A, Dirheimer G (1976) Arginyl-tRNA synthetase from baker's yeast. Purification and some properties. Eur J Biochem 65, 177-82
    • (1976) Eur J Biochem , vol.65 , pp. 177-182
    • Gangloff, J.1    Schutz, A.2    Dirheimer, G.3
  • 23
    • 0025972759 scopus 로고
    • Cysteinyl-tKNA synthetase: Determination of the last E coli aminoacyl-tRNA synthetase primary structure
    • Eriani G, Dirheimer G, Gangloff J (1991) Cysteinyl-tKNA synthetase: determination of the last E coli aminoacyl-tRNA synthetase primary structure. Nucleic Acids Res 19, 265-269
    • (1991) Nucleic Acids Res , vol.19 , pp. 265-269
    • Eriani, G.1    Dirheimer, G.2    Gangloff, J.3
  • 24
    • 0026087217 scopus 로고
    • Sequence determination and modeling of structural motifs for the smallest monomeric aminoacyl-tRNA synthetase
    • Hou YM, Shiba K, Mottes C, Schimmel P (1991) Sequence determination and modeling of structural motifs for the smallest monomeric aminoacyl-tRNA synthetase. Proc Natl Acad Sci USA 88, 976-980
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 976-980
    • Hou, Y.M.1    Shiba, K.2    Mottes, C.3    Schimmel, P.4
  • 27
    • 0028306093 scopus 로고
    • Clustering and co-transcription of the Bacillus subtilis genes encoding the aminoacyl-tRNA synthetases specific for glutamate and for cysteine and the first enzyme for cysteine biosynthesis
    • Gagnon Y, Breton R, Putzer H, Pelchat M, Grunberg-Manago M, Lapointe J (1994) Clustering and co-transcription of the Bacillus subtilis genes encoding the aminoacyl-tRNA synthetases specific for glutamate and for cysteine and the first enzyme for cysteine biosynthesis. J Biol Chem 269, 7473-7482
    • (1994) J Biol Chem , vol.269 , pp. 7473-7482
    • Gagnon, Y.1    Breton, R.2    Putzer, H.3    Pelchat, M.4    Grunberg-Manago, M.5    Lapointe, J.6
  • 28
    • 0028307323 scopus 로고
    • A mutant cysteinyl-tRNA synthetase affecting timing of chromosomal replication initiation in B subtilis and conferring resistance to a protein kinase C inhibitor
    • Séror SJ, Casaregola S, Vannier F, Zouari N, Dahl M, Boye E (1994) A mutant cysteinyl-tRNA synthetase affecting timing of chromosomal replication initiation in B subtilis and conferring resistance to a protein kinase C inhibitor. EMBO J 13, 2472-2480
    • (1994) EMBO J , vol.13 , pp. 2472-2480
    • Séror, S.J.1    Casaregola, S.2    Vannier, F.3    Zouari, N.4    Dahl, M.5    Boye, E.6
  • 29
    • 0018722249 scopus 로고
    • Cysteinyl-tRNA synthetase from Bacillus stearothermophilus. A structural and functional monomer
    • Bruten CJ, Cox LA (1974) Cysteinyl-tRNA synthetase from Bacillus stearothermophilus. A structural and functional monomer. Eur J Biochem 100, 301-308
    • (1974) Eur J Biochem , vol.100 , pp. 301-308
    • Bruten, C.J.1    Cox, L.A.2
  • 30
    • 0030953242 scopus 로고    scopus 로고
    • Microbial pathogencsis: Genomics and beyond
    • Strauss EJ, Falkow S (1997) Microbial pathogencsis: genomics and beyond. Science 276, 707-711
    • (1997) Science , vol.276 , pp. 707-711
    • Strauss, E.J.1    Falkow, S.2
  • 31
    • 0030811859 scopus 로고    scopus 로고
    • Comparative analysis of the genoms of the bacteria Mycoplasma pneumoniae and Mycoplasma genitalium
    • Himmelreich R, Plagens H, Hilhert H, Reiner B, Herrmann R (1997) Comparative analysis of the genoms of the bacteria Mycoplasma pneumoniae and Mycoplasma genitalium. Nucleic Acids Res 25, 701-712
    • (1997) Nucleic Acids Res , vol.25 , pp. 701-712
    • Himmelreich, R.1    Plagens, H.2    Hilhert, H.3    Reiner, B.4    Herrmann, R.5
  • 34
    • 0023202876 scopus 로고
    • Evidence for dispensable sequences inserted into a nucleotide fold
    • Starzyk RM, Webster TA, 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
  • 35
    • 0028108750 scopus 로고
    • Human cytoplasmic isoleucyl-tRNA synthetase: Selective divergence of the anticodon-binding domain and acquisition of a new structural unit
    • Shiba K, Suzuki N, Shigesada K, Namba Y, Schimmel P, Noda T. (1994) Human cytoplasmic isoleucyl-tRNA synthetase: Selective divergence of the anticodon-binding domain and acquisition of a new structural unit. Proc Nutl Acad Sci USA 91, 7435-7439
    • (1994) Proc Nutl Acad Sci USA , vol.91 , pp. 7435-7439
    • Shiba, K.1    Suzuki, N.2    Shigesada, K.3    Namba, Y.4    Schimmel, P.5    Noda, T.6
  • 37
    • 8544270083 scopus 로고    scopus 로고
    • Chromosome 14. The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications
    • Philippsen P et al (1997) Chromosome 14. The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications. Nature 387, 93-98
    • (1997) Nature , vol.387 , pp. 93-98
    • Philippsen, P.1


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