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PMID: 1549561 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

A retroviral-like metal binding motif in an aminoacyl-tRNA synthetase is important for tRNA recognition.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 89 ·No. 6 ·1992-03-15 ·Pages 2032-5

Miller WT, Schimmel P

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.

MeSH Terms
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
Chemicals
Apoenzymes Gene Products, gag Cobalt RNA, Transfer Hydrogen Peroxide Amino Acyl-tRNA Synthetases Alanine-tRNA Ligase Zinc
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Miller W T
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
Schimmel P
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.89.6.2032
Published
1992-03-15
Pages
2032-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC48590
Subset
IM
Grants
NIGMS NIH HHS · GM15539 · United States
NIGMS NIH HHS · GM37641 · United States
External Links
PubMed source DOI: 10.1073/pnas.89.6.2032 PMC Full Text View journal details
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