title: Domain-specific recruitment of amide amino acids for protein synthesis.
abstract: The formation of aminoacyl-transfer RNA is a crucial step in ensuring the accuracy of protein synthesis. Despite the central importance of this process in all living organisms, it remains unknown how archaea and some bacteria synthesize Asn-tRNA and Gln-tRNA. These amide aminoacyl-tRNAs can be formed by the direct acylation of tRNA, catalysed by asparaginyl-tRNA synthetase and glutaminyl-tRNA synthetase, respectively. A separate, indirect pathway involves the formation of mis-acylated Asp-tRNA(Asn) or Glu-tRNA(Gln), and the subsequent amidation of these amino acids while they are bound to tRNA, which is catalysed by amidotransferases. Here we show that all archaea possess an archaea-specific heterodimeric amidotransferase (encoded by gatD and gatE) for Gln-tRNA formation. However, Asn-tRNA synthesis in archaea is divergent: some archaea use asparaginyl-tRNA synthetase, whereas others use a heterotrimeric amidotransferase (encoded by the gatA, gatB and gatC genes). Because bacteria primarily use transamidation, and the eukaryal cytoplasm uses glutaminyl-tRNA synthetase, it appears that the three domains use different mechanisms for Gln-tRNA synthesis; as such, this is the only known step in protein synthesis where all three domains have diverged. Closer inspection of the two amidotransferases reveals that each of them recruited a metabolic enzyme to aid its function; this provides direct evidence for a relationship between amino-acid metabolism and protein biosynthesis.
authors.affiliation: Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114, USA.
authors.forename: D L
authors.initials: DL
authors.lastname: Tumbula
authors.forename: H D
authors.initials: HD
authors.lastname: Becker
authors.forename: W Z
authors.initials: WZ
authors.lastname: Chang
authors.forename: D
authors.initials: D
authors.lastname: Söll
mesh_terms: D000577:Amides / Q000378:metabolism*; D000596:Amino Acids / Q000378:metabolism*; D001105:Archaea / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D004926:Escherichia coli; D017014:Methanobacterium / Q000201:enzymology / Q000235:genetics; D019884:Nitrogenous Group Transferases / Q000235:genetics / Q000378:metabolism*; D010452:Peptide Biosynthesis; D017434:Protein Structure, Tertiary; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*
chemical_list: D000577:Amides; D000596:Amino Acids; D012346:RNA, Transfer, Amino Acyl; D019884:Nitrogenous Group Transferases; C047694:glutamyl-tRNA(Gln) amidotransferase