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Current Opinion in Structural Biology
Volumn 2, Issue 1, 1992, Pages 138-142
Aminoacyl-tRNA synthetases. Current opinion in structural biology 1992, 2:138...-142
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EID: 0000013480     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/0959-440X(92)90189-E     Document Type: Article
Times cited : (31)
References (29)
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    • Schimmel1
  • 3
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    • Crystallographic Study at 2.5 Å Resoltuion of the Interaction of Methionyl-tRNA Synthetase from Escherichia coli with ATP
    • The results of the last refinement of the crystal structure (2.5 Å resolution) of a tryptic fragment of E. coli MetRS complexed with ATP are described. The binding mode of ATP is different from that observed for the tyrosyl-adenylate in TyrRS.
    • (1990) J Mol Biol , vol.216 , pp. 411-424
    • Brunie1    Zelwer2    Risler3
  • 7
  • 9
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    • The Yeast Mitochondrial Leucyl-tRNA Synthetase is a Splicing Factor for the Excision of Several Group I Introns
    • (1990) Mol Gen Genet , vol.224 , pp. 209-221
    • Labouesse1
  • 10
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    • A Mammalian Tryptophanyl-tRNA Synthetase Shows Little Homology to Prokaryotic Synthetases but Near Identity with Mammalian Peptide Chain Release Factor
    • The amino acid sequence of beef pancreatic TrpRS is determined. Its sequence identity with prokaryotic and yeast mitochondrial TrpRS is low and limited to the consensus sequence regions; however, 90% identity is observed with the rabbit peptide-chain release factor.
    • (1991) Biochemistry , vol.30 , pp. 7809-7817
    • Garret1    Pajot2    Trezeguet3    Labouesse4    Merle5    Gandar6    Benedetto7    Sallafranque8    Alterio9    Gueguen10
  • 11
    • 0026429275 scopus 로고
    • Asp
    • Asp-AspRS from yeast is described. The active-site domain with the three characteristic signature motifs that are conserved in eight class-I synthetases is analyzed. Interactions with the tRNA are shown to be significantly different from those observed in the class-I E. coli GlnRS system.
    • (1991) Science , vol.252 , pp. 1682-1689
    • Ruff1    Krishnaswamy2    Boeglin3    Poterszman4    Mitschler5    Podjarny6    Rees7    Thierry8    Moras9
  • 12
    • 0025744320 scopus 로고
    • Structural Basis of Anticodon Loop Recognition by Glutaminyl-tRNA Synthetase
    • Gln and the interactions made with GlnRS are described. The anticodon stem is extended by two non-Watson-Crick base pairs. The three anticodon bases bind to three separate pockets in the protein.
    • (1991) Nature , vol.352 , pp. 213-218
    • Rould1    Perona2    Steitz3
  • 13
    • 0025771974 scopus 로고
    • Structural Similarities in Glutaminyl- and Methionyl-tRNA Synthetase Suggest a Common Overall Orientation of tRNA Binding
    • The structures of E. coli GlnRS and MetRS are compared, revealing significant similarities. This analysis suggests a similar binding mode of the tRNAs to their respective synthetases.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 2903-2907
    • Perona1    Rould2    Steitz3    Risler4    Zelwer5    Brunie6
  • 14
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    • Aspartyl-tRNA Synthetase from Escherichia coli: Cloning and Characterization of the Gene, Homologies of its Translated Amino Acid Sequence with Asparaginyl- and Lysyl-tRNA Synthetases
    • The amino acid sequence of E. coli AspRS is analyzed in terms of sequence identity with four enzymes of other species and with the subgroup-related AsnRS and LysRS. Conserved motifs and additional important residues are noted.
    • (1990) Nucleic Acids Res , vol.18 , pp. 7109-7118
    • Eriani1    Dirheimer2    Gangloff3
  • 15
    • 0025731710 scopus 로고
    • Identification of Structurally and Functionally Important Histidine Residues to Cytoplasmic Aspartyl-tRNA Synthetase from Saccharomyces cerevisiae
    • A combination of chemical labelling using diethyl pyrocarbonate and site-directed mutagenesis leads to the identification of three histidines of yeast AspRS that are important for catalytic activity (one residue) or structural integrity (two residues).
    • (1991) Biochemistry , vol.30 , pp. 4284-4289
    • Gasparini1    Vincendon2    Eriani3    Gangloff4    Boulanger5    Reinbolt6    Kern7
  • 17
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    • Structure and Evolution of a Group of Related Aminoactyl-tRNA Synthetases
    • The primary sequence of LysRS from yeast mitochondria is presented. High sequence identities with AspRS and AsnRS are noted and significant identity with AsnRS is also observed.
    • (1991) J Mol Biol , vol.218 , pp. 557-568
    • Gatti1    Tzagoloff2
  • 18
    • 0025874160 scopus 로고
    • Sequence, Structural and Evolutionary Relationships Between Class 2 Aminoacyl-tRNA Synthetases
    • 2 dimeric synthetases into the two aminoacyl-RS classes is analyzed. In the case of AlaRS where only one out of the three characteristic structural motifs had previously been detected, the second one is convincingly aligned.
    • (1991) Nucleic Acids Res , vol.19 , pp. 3489-3498
    • Cusack1    Härtlein2    Leberman3
  • 20
    • 0026032475 scopus 로고
    • Assembly of a Class I tRNA Synthetase from Products of an Artificially Split Gene
    • Met can be recognized and charged both in vivo and in vitro.
    • (1991) Biochemistry , vol.30 , pp. 319-324
    • Burbaum1    Schimmel2
  • 22
    • 0026059951 scopus 로고
    • Lysine 335, Part of the KMSKS Signature Sequence, Plays a Crucial Role in the Amino Acid Activation Catalysed by the Methionyl-tRNA Synthetase from Escherichia coli
    • The role of the essential residue Lys335 is investigated by site-directed mutagenesis and pre-steady state analysis of methionyladenylate synthesis. It is shown that the N6 amino group of this residue stabilizes the transient complex of MetRS with methionine.
    • (1991) J Mol Biol , vol.217 , pp. 465-474
    • Mechulam1    Dardel2    Le Corre3    Blanquet4    Fayat5
  • 23
    • 0025787133 scopus 로고
    • Identification of Potential Amino Acid Residues Supporting Anticodon Recognition in Yeast Methionyl-tRNA Synthetase
    • Site-directed mutagenesis experiments indicate that the side chains of Asn584 and Arg588 could be involved in a direct interaction with the tRNA anticodon.
    • (1991) FEBS Lett , vol.289 , pp. 217-220
    • Despons1    Walter2    Senger3    Ebel4    Fasiolo5
  • 24
    • 0025972759 scopus 로고
    • Cysteinyl-tRNA Synthetase: Determination of the Last E. coli Aminoacyl-tRNA Synthetase Primary Structure
    • This paper presents the cloning, sequencing and sequence analysis of CysRS: this is the 20th and the last system for which a primary sequence is now available. The enzyme belongs to class I and exhibits large sequence identity with MetRS. Significant sequence identities with Ile-, Leu- and ValRS are also demonstrated.
    • (1991) Nucleic Acids Res , vol.19 , pp. 265-269
    • Eriani1    Dirheimer2    Gangloff3
  • 25
    • 0026087217 scopus 로고
    • Sequence Determination and Modeling of Structural Motifs for the Smallest Monomeric Aminoacyl-tRNA Synthetase
    • This paper describes an independent sequence determination and the subsequent model analysis of E. coli CysRS, the smallest of the aminoacyl-RS family.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 976-980
    • Hou1    Shiba2    Mottes3    Schimmel4
  • 26
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    • Evolution of Aminoacyl-tRNA Synthetase Quaternary Structure and Activity: Saccharomyces cerevisiae Mitochondrial Phenylalanyl-tRNA Synthetase
    • A single yeast mitochondrial polypeptide is an active PheRS in a monomeric form.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8387-8391
    • Sanni1    Walter2    Boulanger3    Ebel4    Fasiolo5
  • 27
    • 0025028914 scopus 로고
    • Evidence for 2 Types of Complexes Formed by Yeast Tyrosyl-transfer RNA Synthetase with Cognate and Non-cognate Transfer RNA …-Effect of Ribonucleoside Triphosphates
    • (1990) Eur J Biochem , vol.193 , pp. 783-788
    • Rubelj1    Weyganddurasevic2    Kucan3
  • 28
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    • Recognition of Escherichia coli Valine Transfer RNA by its Cognate Synthetase …- a Fluorine-19 NMR Study
    • (1991) J Biochem , vol.30 , pp. 1655-1663
    • Chu1    Horowitz2
  • 29
    • 0025877055 scopus 로고
    • Mutant Aminoacyl-transfer RNA Synthetase that Compensates for a Mutation in the Major Identity Determinant of its Transfer RNA
    • A single amino acid substitution in AlaRS is sufficient to compensate for mutation in the major determinant, G3-U70, of the cognate tRNA.
    • (1991) Biochemistry , vol.30 , pp. 2635-2641
    • Miller1    Hou2    Schimmel3

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.