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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 |
|---|---|
| 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: |
| author_facet |
Roy, Hervé Becker, Hubert Dominique Reinbolt, Joseph Kern, Daniel Roy, Hervé Becker, Hubert Dominique Reinbolt, Joseph Kern, Daniel |
|---|---|
| author |
Roy, Hervé Becker, Hubert Dominique Reinbolt, Joseph Kern, Daniel |
| spellingShingle |
Roy, Hervé Becker, Hubert Dominique Reinbolt, Joseph Kern, Daniel Proceedings of the National Academy of Sciences When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism Multidisciplinary |
| author_sort |
roy, hervé |
| spelling |
Roy, Hervé Becker, Hubert Dominique Reinbolt, Joseph Kern, Daniel 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.1632156100 <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> When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism Proceedings of the National Academy of Sciences |
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| title |
When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism |
| title_unstemmed |
When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism |
| title_full |
When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism |
| title_fullStr |
When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism |
| title_full_unstemmed |
When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism |
| title_short |
When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism |
| title_sort |
when contemporary aminoacyl-trna synthetases invent their cognate amino acid metabolism |
| topic |
Multidisciplinary |
| url |
http://dx.doi.org/10.1073/pnas.1632156100 |
| publishDate |
2003 |
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9837-9842 |
| description |
<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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| author | Roy, Hervé, Becker, Hubert Dominique, Reinbolt, Joseph, Kern, Daniel |
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| description | <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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| imprint_str_mv | Proceedings of the National Academy of Sciences, 2003 |
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| spelling | Roy, Hervé Becker, Hubert Dominique Reinbolt, Joseph Kern, Daniel 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.1632156100 <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> When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism Proceedings of the National Academy of Sciences |
| spellingShingle | Roy, Hervé, Becker, Hubert Dominique, Reinbolt, Joseph, Kern, Daniel, Proceedings of the National Academy of Sciences, When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism, Multidisciplinary |
| title | When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism |
| title_full | When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism |
| title_fullStr | When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism |
| title_full_unstemmed | When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism |
| title_short | When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism |
| title_sort | when contemporary aminoacyl-trna synthetases invent their cognate amino acid metabolism |
| title_unstemmed | When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism |
| topic | Multidisciplinary |
| url | http://dx.doi.org/10.1073/pnas.1632156100 |