PMID:1379318
| Citation |
Miller, WT and Schimmel, P (1992) A metal-binding motif implicated in RNA recognition by an aminoacyl-tRNA synthetase and by a retroviral gene product. Mol. Microbiol. 6:1259-62 |
|---|---|
| Abstract |
A randomly generated mutation in Escherichia coli alanine tRNA synthetase compensates for a mutation in its cognate tRNA. The enzyme's mutation occurs next to a Cys-X2-Cys-X6-His-X2-His metal-binding motif that is distinct from the zinc finger motif found in some DNA-binding proteins. Instead, the synthetase's metal binding domain resembles the Cys-X2-Cys-X4-His-X4-Cys metal-binding domain of the gag gene product of retroviruses. For Ala-tRNA synthetase, the metal bound at the Cys-His motif is important specifically for the tRNA-dependent step of catalysis, and the enzyme-tRNA interaction is dependent on the geometry of metal co-ordination to the enzyme. These data, and the demonstrated sensitivity of RNA packaging to mutations in the metal-binding domain of the gag gene product of retroviruses, suggest that an aminoacyl-tRNA synthetase and retroviruses have adopted a related metal-binding motif for RNA recognition. |
| Links | |
| Keywords |
Alanine-tRNA Ligase/genetics; Alanine-tRNA Ligase/metabolism; Allosteric Regulation; Allosteric Site; Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cobalt/metabolism; Consensus Sequence; Escherichia coli/genetics; Gene Products, gag/genetics; Gene Products, gag/metabolism; Genes, Bacterial; Genes, gag; Molecular Sequence Data; Mutation; RNA, Bacterial/genetics; RNA, Bacterial/metabolism; RNA, Transfer, Ala/genetics; RNA, Transfer, Ala/metabolism; Retroviridae/genetics; Zinc/metabolism |
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