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PMID: 10922054 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Hydrolytic editing by a class II aminoacyl-tRNA synthetase.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 97 ·No. 16 ·2000-08-01 ·Pages 8916-20

Beuning PJ, Musier-Forsyth K

Abstract

Editing reactions catalyzed by aminoacyl-tRNA synthetases are critical for accurate translation of the genetic code. To date, this activity, whereby misactivated amino acids are hydrolyzed either before or after transfer to noncognate tRNAs, has been characterized extensively only in the case of class I synthetases. Class II synthetases have an active-site architecture that is completely distinct from that of class I. Thus, findings on editing by class I synthetases may not be applicable generally to class II enzymes. Class II Escherichia coli proline-tRNA synthetase is shown here to misactivate alanine and to hydrolyze the noncognate amino acid before transfer to tRNA(Pro). This enzyme also is capable of rapidly deacylating a mischarged Ala-tRNA(Pro) variant. A single cysteine residue (C443) that is located within the class II-specific motif 3 consensus sequence was shown previously to be dispensable for proline-tRNA synthetase aminoacylation activity. We show here that C443 is critical for the hydrolytic editing of Ala-tRNA(Pro) by this class II synthetase.

MeSH Terms
Amino Acyl-tRNA Synthetases/chemistry,metabolism Cysteine/metabolism Escherichia coli/enzymology Hydrolysis RNA Editing
Chemicals
Amino Acyl-tRNA Synthetases Cysteine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Beuning P J
Department of Chemistry, University of Minnesota, 207 Pleasant Street Southeast, Minneapolis, MN 55455, USA.
Musier-Forsyth K
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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.97.16.8916
Published
2000-08-01
Pages
8916-20
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC16796
Subset
IM
Grants
NIGMS NIH HHS · R01 GM049928 · United States
NIGMS NIH HHS · GM42298 · United States
External Links
PubMed source DOI: 10.1073/pnas.97.16.8916 PMC Full Text View journal details
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