Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0039483 (giant cell arteritis)
 3,204 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The recognition of transfer RNAs (tRNAs) by aminoacyl tRNA synthetases is a critical step in establishing the fidelity of translation. For E. coli cysteine tRNA synthetase, recognition of tRNA(Cys) and discrimination from all other tRNAs is based on the U73 discriminator base, the GCA anticodon, and a G15:G48 tertiary base pair. While the discriminator base and the anticodon sequence are often used by many synthetases as the determinants for tRNA recognition, the dependence on a tertiary interaction in the cognate tRNA for recognition is unique to the cysteine enzyme. Here the structural basis for recognition at the G15:G48 tertiary interaction of E. coli tRNA(Cys) is explored by structural modeling, chemical modifications, and kinetic analysis. The results established an unusual RNA tertiary interaction that provides a plausible mechanism for recognition by cysteine tRNA synthetase.
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PMID:RNA recognition based on a pair of tertiary hydrogen interaction. 864 62

The crystal structure of Escherichia coli cysteinyl-tRNA synthetase (CysRS) bound to tRNA(Cys) at a resolution of 2.3 A reveals base-specific and shape-selective interactions across an extensive protein-RNA recognition interface. The complex contains a mixed alpha/beta C-terminal domain, which is disordered in the unliganded enzyme. This domain makes specific hydrogen bonding interactions with all three bases of the GCA anticodon. The tRNA anticodon stem is bent sharply toward the enzyme as compared with its conformation when bound to elongation factor Tu, providing an essential basis for shape-selective recognition. The CysRS structure also reveals interactions of conserved enzyme groups with the sugar-phosphate backbone in the D loop, adjacent to an unusual G15.G48 tertiary base pair previously implicated in tRNA aminoacylation. A combined mutational analysis of enzyme and tRNA groups at G15.G48 supports the notion that contacts between CysRS and the sugar-phosphate backbone contribute to recognition by indirect readout.
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PMID:Shape-selective RNA recognition by cysteinyl-tRNA synthetase. 1548 61