PMID:1549561

Citation	Miller, WT and Schimmel, P (1992) A retroviral-like metal binding motif in an aminoacyl-tRNA synthetase is important for tRNA recognition. Proc. Natl. Acad. Sci. U.S.A. 89:2032-5
Abstract	The gag genes of retroviruses encode nucleocapsid proteins that package genomic RNA and are essential for viral infectivity. These RNA binding proteins have a Cys-Xaa2-Cys-Xaa4-His-Xaa4-Cys zinc binding motif that is distinct from the typical zinc-finger motif Cys-Xaa2-Cys-Xaa12-14-His-Xaa2-His that is found in some transcriptional activators. Escherichia coli alanyl-tRNA synthetase contains a zinc-binding Cys-Xaa2-Cys-Xaa6-His-Xaa2-His motif that resembles that of retroviral nucleic acid binding proteins. We show here that, for alanyl-tRNA synthetase, the metal bound at the retroviral-like metal binding motif is important specifically for tRNA recognition and not for amino acid activation. Moreover, the enzyme-tRNA interaction is strongly dependent on the geometry of metal coordination to the protein. These and additional experiments collectively suggest a role for the retroviral-like metal binding motif in RNA recognition and, further, raise the possibility that the protein-bound metal itself participates in an RNA interaction.
Links	PubMed PMC48590
Keywords	Alanine-tRNA Ligase/metabolism; Amino Acyl-tRNA Synthetases/metabolism; Apoenzymes/metabolism; Binding Sites; Cobalt/pharmacology; Escherichia coli/enzymology; Gene Products, gag/metabolism; Hydrogen Peroxide/pharmacology; Kinetics; RNA, Transfer/metabolism; Substrate Specificity; Zinc/pharmacology
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
ECO24:SYA	enables	GO:0004813: alanine-tRNA ligase activity	ECO:0000314: direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
ECO24:SYA		GO:0004813: alanine-tRNA ligase activity	ECO:0000314:		F		Figures 1,2.	complete CACAO 3132

References

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