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When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism
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| Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
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| Personen und Körperschaften: | , , , |
| In: | Proceedings of the National Academy of Sciences, 100, 2003, 17, S. 9837-9842 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Proceedings of the National Academy of Sciences
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| Schlagwörter: |
| Zusammenfassung: | <jats:p> 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 <jats:italic>Pyrococcus abyssi</jats:italic> AsnRS2, in contrast to AsnRS, does not sustain asparaginyl-tRNA <jats:sup>Asn</jats:sup> synthesis but is instead capable of converting aspartic acid into asparagine. Functional analysis and complementation of an <jats:italic>Escherichia coli</jats:italic> 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. </jats:p> |
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| Umfang: | 9837-9842 |
| ISSN: |
0027-8424
1091-6490 |
| DOI: | 10.1073/pnas.1632156100 |