The Amino Acid Sequence of the Tyrosy1-tRNA Synthetase from Bacillus stearothermophilus

作者：Greg P. Winter, Gordon L. E. Koch, Brian Selby Hartley, David George Barker · 发表于：European Journal of Biochemistry · 年份：1983 · DOI：10.1111/j.1432-1033.1983.tb07374.x · 被引用次数：112 · 研究领域：RNA and protein synthesis mechanisms、Bacterial Genetics and Biotechnology、Chemical Synthesis and Analysis

The primary structure of the tyrosyl-tRNA synthetase (TyrTS) of Bacillus stearothermophilus has been deduced from the nucleotide sequence of the cloned gene and from the amino acid sequence of peptides isolated from the purified enzyme. TyrTS (B. stearothermophilus) has a molecular weight of 47316 and the sequence is 56% homologous with that of TyrTS (Escherichia coli). The binding domain for the substrate intermediate tyrosyl adenylate is located in the N-terminal portion of the polypeptide and is highly conserved in both enzymes. Several lysine residues, which are shielded from acetylation in the TyrTS-tRNATyr complex, are also located in a stretch of highly conserved sequence.