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

Sheppard, K.; Yuan, J.; Hohn, M. J.; Jester, B.; Devine, K. M.; Soll, D.

doi:10.1093/nar/gkn015

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

Journal Article · Tue Feb 05 00:00:00 EST 2008 · Nucleic Acids Research

DOI:https://doi.org/10.1093/nar/gkn015· OSTI ID:1625436

Sheppard, K. ^[1]; Yuan, J. ^[2]; Hohn, M. J. ^[2]; Jester, B. ^[3]; Devine, K. M. ^[3]; Soll, D. ^[4]

Yale Univ., New Haven, CT (United States). Depts. of Molecular Biophysics and Biochemsitry; DOE/OSTI
Yale Univ., New Haven, CT (United States). Depts. of Molecular Biophysics and Biochemsitry
Trinity College Dublin (Ireland). Smurfit Inst. of Genetics
Yale Univ., New Haven, CT (United States). Depts. of Molecular Biophysics and Biochemsitry; Yale Univ., New Haven, CT (United States). Dept. of Chemistry

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 tRNAdependent 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 tRNAdependent 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 SectRNA synthesis, O-phosphoseryl-tRNA kinase phosphorylates Ser-tRNA to form the intermediate which is then modified to Sec-tRNA by SeptRNA: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.

View Accepted Manuscript (DOE)

Research Organization:: Yale Univ., New Haven, CT (United States)

Sponsoring Organization:: Enterprise Ireland; European Commission (EC); National Institutes of Health (NIH); USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division

OSTI ID:: 1625436

Journal Information:: Nucleic Acids Research, Journal Name: Nucleic Acids Research Journal Issue: 6 Vol. 36; ISSN 0305-1048

Publisher:: Oxford University PressCopyright Statement

Country of Publication:: United States

Language:: English

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