Emergence and Evolution

被引:39
作者
Bullwinkle, Tammy J. [1 ]
Ibba, Michael [1 ]
机构
[1] Ohio State Univ, Dept Microbiol, Columbus, OH 43210 USA
来源
AMINOACYL-TRNA SYNTHETASES IN BIOLOGY AND MEDICINE | 2014年 / 344卷
关键词
aaRS; Amino acid; Aminoacyl-tRNA synthetase; Enzyme specificity; Proofreading; Transamidation; Translation; tRNA; TRANSFER-RNA-SYNTHETASE; PHENYLALANYL-TRANSFER-RNA; ASPARTYL-TRANSFER-RNA; COMPLETE GENOME SEQUENCE; AMINO-ACID ACTIVATION; DEPENDENT CYSTEINE BIOSYNTHESIS; ANGSTROM CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; CLASS-I; THERMUS-THERMOPHILUS;
D O I
10.1007/128_2013_423
中图分类号
R914 [药物化学];
学科分类号
100701 ;
摘要
The aminoacyl-tRNA synthetases (aaRSs) are essential components of the protein synthesis machinery responsible for defining the genetic code by pairing the correct amino acids to their cognate tRNAs. The aaRSs are an ancient enzyme family believed to have origins that may predate the last common ancestor and as such they provide insights into the evolution and development of the extant genetic code. Although the aaRSs have long been viewed as a highly conserved group of enzymes, findings within the last couple of decades have started to demonstrate how diverse and versatile these enzymes really are. Beyond their central role in translation, aaRSs and their numerous homologs have evolved a wide array of alternative functions both inside and outside translation. Current understanding of the emergence of the aaRSs, and their subsequent evolution into a functionally diverse enzyme family, are discussed in this chapter.
引用
收藏
页码:43 / 87
页数:45
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