PMID:9478190
| Citation |
Musier-Forsyth, K, Stehlin, C, Burke, B and Liu, H' (1997) Understanding species-specific differences in substrate recognition by Escherichia coli and human prolyl-tRNA synthetases. Nucleic Acids Symp. Ser. ':5-7 |
|---|---|
| Abstract |
Class II human prolyl-tRNA synthetase (ProRS) aminoacylates in vitro transcribed human tRNA(Pro) with kinetic parameters that are similar to those previously determined for aminoacylation of Escherichia coli tRNA(Pro) by its cognate synthetase. As in the bacterial system, large decreases in aminoacylation by human ProRS occur upon mutating anticodon positions G35 and G36 of human tRNA(Pro). The N73 'discriminator' base and the first and third base pairs of the acceptor stem vary between the E.coli and human isoacceptor groups. In contrast to the E. coli synthetase, the human enzyme does not appear to recognize these elements, since mutations at these positions do not significantly affect cognate synthetase charging. E. coli ProRS does not cross-aminoacylate human tRNA(Pro), and the bacterial tRNA(Pro) is a poor substrate for the human enzyme. Mutations in both the tRNAs and the synthetases have been made in an effort to identify elements in each system responsible for blocking cross-species aminoacylation. Alignment of all known ProRS primary sequences from different species reveals particularly low overall sequence homology, as well as two distinct groups of enzymes. The sequence divergence between E. coli and human ProRSs helps to explain the species-specific differences in the RNA code for aminoacylation of tRNA(Pro). |
| Links | |
| Keywords |
Amino Acid Sequence; Amino Acyl-tRNA Synthetases/metabolism; Base Sequence; Escherichia coli/enzymology; Humans; Molecular Sequence Data; Nucleic Acid Conformation; RNA, Transfer, Amino Acyl/metabolism; Species Specificity; Structure-Activity Relationship |
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