Abstract:
:The aminoacyl-tRNA synthetases are an ancient group of enzymes that catalyze the covalent attachment of an amino acid to its cognate transfer RNA. The question of specificity, that is, how each synthetase selects the correct individual or isoacceptor set of tRNAs for each amino acid, has been referred to as the second genetic code. A wealth of structural, biochemical, and genetic data on this subject has accumulated over the past 40 years. Although there are now crystal structures of sixteen of the twenty synthetases from various species, there are only a few high resolution structures of synthetases complexed with cognate tRNAs. Here we review briefly the structural information available for synthetases, and focus on the structural features of tRNA that may be used for recognition. Finally, we explore in detail the insights into specific recognition gained from classical and atomic group mutagenesis experiments performed with tRNAs, tRNA fragments, and small RNAs mimicking portions of tRNAs.
journal_name
Biopolymersjournal_title
Biopolymersauthors
Beuning PJ,Musier-Forsyth Kdoi
10.1002/(SICI)1097-0282(1999)52:1<1::AID-BIP1>3.0.subject
Has Abstractpub_date
1999-01-01 00:00:00pages
1-28issue
1eissn
0006-3525issn
1097-0282pii
10.1002/(SICI)1097-0282(1999)52:1<1::AID-BIP1>3.0.journal_volume
52pub_type
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