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PMID: 18252769 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Review

From one amino acid to another: tRNA-dependent amino acid biosynthesis.

Nucleic acids research ·Vol. 36 ·No. 6 ·2008-04-00 ·Pages 1813-25

Sheppard K, Yuan J, Hohn MJ, Jester B, Devine KM, Söll D

Abstract

Aminoacyl-tRNAs (aa-tRNAs) are the essential substrates for translation. Most aa-tRNAs are formed by direct aminoacylation of tRNA catalyzed by aminoacyl-tRNA synthetases. However, a smaller number of aa-tRNAs (Asn-tRNA, Gln-tRNA, Cys-tRNA and Sec-tRNA) are made by synthesizing the amino acid on the tRNA by first attaching a non-cognate amino acid to the tRNA, which is then converted to the cognate one catalyzed by tRNA-dependent modifying enzymes. Asn-tRNA or Gln-tRNA formation in most prokaryotes requires amidation of Asp-tRNA or Glu-tRNA by amidotransferases that couple an amidase or an asparaginase to liberate ammonia with a tRNA-dependent kinase. Both archaeal and eukaryotic Sec-tRNA biosynthesis and Cys-tRNA synthesis in methanogens require O-phosophoseryl-tRNA formation. For tRNA-dependent Cys biosynthesis, O-phosphoseryl-tRNA synthetase directly attaches the amino acid to the tRNA which is then converted to Cys by Sep-tRNA: Cys-tRNA synthase. In Sec-tRNA synthesis, O-phosphoseryl-tRNA kinase phosphorylates Ser-tRNA to form the intermediate which is then modified to Sec-tRNA by Sep-tRNA:Sec-tRNA synthase. Complex formation between enzymes in the same pathway may protect the fidelity of protein synthesis. How these tRNA-dependent amino acid biosynthetic routes are integrated into overall metabolism may explain why they are still retained in so many organisms.

MeSH Terms
Amino Acyl-tRNA Synthetases/chemistry,metabolism Asparagine/biosynthesis Cysteine/biosynthesis Glutamine/biosynthesis Nitrogenous Group Transferases/chemistry,metabolism Phosphotransferases/chemistry,metabolism RNA, Transfer, Amino Acyl/metabolism Selenocysteine/biosynthesis
Chemicals
RNA, Transfer, Amino Acyl glutamyl-tRNA(Gln) selenocysteinyl-tRNA Selenocysteine Glutamine Asparagine Nitrogenous Group Transferases Phosphotransferases Amino Acyl-tRNA Synthetases Cysteine
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Sheppard Kelly
Department of Molecular Biophysics, Yale University, New Haven, CT 06520-8114, USA.
Yuan Jing
Hohn Michael J
Jester Brian
Devine Kevin M
Söll Dieter
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Article Info
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Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
1362-4962
DOI
10.1093/nar/gkn015
Published
2008-04-00
Epub
2008-00-05
Pages
1813-25
Language
English
Region
England
NLM ID
0411011
PMCID
PMC2330236
Subset
IM
Grants
NIGMS NIH HHS · R01 GM022854 · United States
NIGMS NIH HHS · R37 GM022854 · United States
NIGMS NIH HHS · GM22854 · United States
External Links
PubMed source DOI: 10.1093/nar/gkn015 PMC Full Text View journal details
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