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PMID: 9789001 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Glutamyl-tRNA(Gln) amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 95 ·No. 22 ·1998-10-27 ·Pages 12838-43

Curnow AW, Tumbula DL, Pelaschier JT, Min B, Söll D

Abstract

Asparaginyl-tRNA (Asn-tRNA) and glutaminyl-tRNA (Gln-tRNA) are essential components of protein synthesis. They can be formed by direct acylation by asparaginyl-tRNA synthetase (AsnRS) or glutaminyl-tRNA synthetase (GlnRS). The alternative route involves transamidation of incorrectly charged tRNA. Examination of the preliminary genomic sequence of the radiation-resistant bacterium Deinococcus radiodurans suggests the presence of both direct and indirect routes of Asn-tRNA and Gln-tRNA formation. Biochemical experiments demonstrate the presence of AsnRS and GlnRS, as well as glutamyl-tRNA synthetase (GluRS), a discriminating and a nondiscriminating aspartyl-tRNA synthetase (AspRS). Moreover, both Gln-tRNA and Asn-tRNA transamidation activities are present. Surprisingly, they are catalyzed by a single enzyme encoded by three ORFs orthologous to Bacillus subtilis gatCAB. However, the transamidation route to Gln-tRNA formation is idled by the inability of the discriminating D. radiodurans GluRS to produce the required mischarged Glu-tRNAGln substrate. The presence of apparently redundant complete routes to Asn-tRNA formation, combined with the absence from the D. radiodurans genome of genes encoding tRNA-independent asparagine synthetase and the lack of this enzyme in D. radiodurans extracts, suggests that the gatCAB genes may be responsible for biosynthesis of asparagine in this asparagine prototroph.

MeSH Terms
Acylation Amino Acyl-tRNA Synthetases/metabolism Asparagine/biosynthesis Cloning, Molecular DNA, Bacterial/chemistry,genetics Genome, Bacterial Glutamate-tRNA Ligase/metabolism Gram-Positive Cocci/enzymology,genetics Kinetics Models, Chemical Nitrogenous Group Transferases/metabolism Open Reading Frames
Chemicals
DNA, Bacterial Asparagine Nitrogenous Group Transferases glutamyl-tRNA(Gln) amidotransferase Amino Acyl-tRNA Synthetases Glutamate-tRNA Ligase glutaminyl-tRNA synthetase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Curnow A W
Department of Molecular Biophysics and Biochemistry, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520-8114, USA.
Tumbula D L
Pelaschier J T
Min B
Söll D
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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.95.22.12838
Published
1998-10-27
Pages
12838-43
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC23620
Subset
IM
Grants
NIGMS NIH HHS · R37 GM022854 · United States
NIGMS NIH HHS · GM55674 · United States
NIGMS NIH HHS · R01 GM022854 · United States
NIGMS NIH HHS · GM22854 · United States
NIGMS NIH HHS · F32 GM019278 · United States
External Links
PubMed source DOI: 10.1073/pnas.95.22.12838 PMC Full Text View journal details
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