Primary Structure of a Large Aminoacyl-tRNA Synthetase
- 25 September 1981
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 213 (4515), 1497-1501
- https://doi.org/10.1126/science.7025207
Abstract
The complete primary structure of Escherichia coli alanyl-tRNA synthetase, a 95,000-dalton polypeptide, was established by sequencing the gene encoding the enzyme and by sequencing oligopeptides in hydrolysates of the protein by gas chromatography-mass spectrometry. Contrary to expectation, this long polypeptide contains no lengthy duplications. One 13-residue peptide is homologous with E. coli tyrosyl-tRNA synthetase, and clusters of charged amino acids occur in several sections of the structure.This publication has 18 references indexed in Scilit:
- An aminoacyl tRNA synthetase binds to a specific DNA sequence and regulates its gene transcriptionNature, 1981
- DNA sequence analysis of the transposon Tn3: Three genes and three sites involved in transposition of Tn3Cell, 1979
- Transposition protein of Tn3: identification and characterisation of an essential represser-controlled gene productNature, 1979
- Mass spectrometric sequencing of peptides and proteinsPublished by Walter de Gruyter GmbH ,1978
- Phenylalanyl‐tRNA synthetase from baker's yeast Repeated sequences in the two subunitsFEBS Letters, 1977
- The amino acid sequence of tryptophanyl tRNA Synthetase from Bacillus stearothermophilusFEBS Letters, 1977
- Studies of the binding sites of Escherichia coli ribosomal protein S7 with 16S RNA by ultraviolet irradiationFEBS Letters, 1976
- Repeated sequences in methionyl‐tRNA synthetase from E. coliFEBS Letters, 1974
- Repeating sequences in aminoacyl-tRNA synthetasesNature, 1974
- Structural studies on isoleucyl‐tRNA synthetase from E. coliFEBS Letters, 1973