PMID- 12874385
OWN - NLM
STAT- MEDLINE
DCOM- 20031029
LR  - 20181113
IS  - 0027-8424 (Print)
IS  - 1091-6490 (Electronic)
IS  - 0027-8424 (Linking)
VI  - 100
IP  - 17
DP  - 2003 Aug 19
TI  - When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid 
      metabolism.
PG  - 9837-42
AB  - Faithful protein synthesis relies on a family of essential enzymes called 
      aminoacyl-tRNA synthetases, assembled in a piecewise fashion. Analysis of the 
      completed archaeal genomes reveals that all archaea that possess asparaginyl-tRNA 
      synthetase (AsnRS) also display a second ORF encoding an AsnRS truncated from its 
      anticodon binding-domain (AsnRS2). We show herein that Pyrococcus abyssi AsnRS2, 
      in contrast to AsnRS, does not sustain asparaginyl-tRNAAsn synthesis but is 
      instead capable of converting aspartic acid into asparagine. Functional analysis 
      and complementation of an Escherichia coli asparagine auxotrophic strain show 
      that AsnRS2 constitutes the archaeal homologue of the bacterial ammonia-dependent 
      asparagine synthetase A (AS-A), therefore named archaeal asparagine synthetase A 
      (AS-AR). Primary sequence- and 3D-based phylogeny shows that an archaeal AspRS 
      ancestor originated AS-AR, which was subsequently transferred into bacteria by 
      lateral gene transfer in which it underwent structural changes producing AS-A. 
      This study provides evidence that a contemporary aminoacyl-tRNA synthetase can be 
      recruited to sustain amino acid metabolism.
FAU - Roy, Herve
AU  - Roy H
AD  - Departement Mecanismes et Macromolecules de la Synthese Proteique et 
      Cristallogenese, UPR 9002, Institut de Biologie Moleculaire et Cellulaire du 
      Centre National de la Recherche Scientifique, 15 Rue Rene Descartes, F-67084 
      Strasbourg Cedex, France.
FAU - Becker, Hubert Dominique
AU  - Becker HD
FAU - Reinbolt, Joseph
AU  - Reinbolt J
FAU - Kern, Daniel
AU  - Kern D
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20030721
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Amino Acids)
RN  - 0 (RNA, Transfer, Amino Acyl)
RN  - EC 6.1.1.- (Amino Acyl-tRNA Synthetases)
RN  - EC 6.1.1.12 (Aspartate-tRNA Ligase)
RN  - EC 6.1.1.22 (asparaginyl-tRNA synthetase)
SB  - IM
CIN - Proc Natl Acad Sci U S A. 2003 Aug 19;100(17):9650-2. PMID: 12913115
MH  - Amino Acid Sequence
MH  - Amino Acids/*metabolism
MH  - Amino Acyl-tRNA Synthetases/chemistry/genetics/*metabolism
MH  - *Aspartate-tRNA Ligase
MH  - Catalytic Domain/genetics
MH  - Cloning, Molecular
MH  - Escherichia coli/genetics/metabolism
MH  - Genes, Archaeal
MH  - Genes, Bacterial
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Phylogeny
MH  - Protein Conformation
MH  - Pyrococcus/enzymology/genetics
MH  - *RNA, Transfer, Amino Acyl
MH  - Sequence Homology, Amino Acid
MH  - Substrate Specificity
PMC - PMC187858
EDAT- 2003/07/23 05:00
MHDA- 2003/10/30 05:00
PMCR- 2004/02/19
CRDT- 2003/07/23 05:00
PHST- 2003/07/23 05:00 [pubmed]
PHST- 2003/10/30 05:00 [medline]
PHST- 2003/07/23 05:00 [entrez]
PHST- 2004/02/19 00:00 [pmc-release]
AID - 1632156100 [pii]
AID - 1009837 [pii]
AID - 10.1073/pnas.1632156100 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 2003 Aug 19;100(17):9837-42. doi: 
      10.1073/pnas.1632156100. Epub 2003 Jul 21.