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The Predatory Bacterium Bdellovibrio bacteriovorus Aspartyl-tRNA Synthetase Recognizes tRNA(Asn) as a Substrate
The predatory bacterium Bdellovibrio bacteriovorus preys on other Gram-negative bacteria and was predicted to be an asparagine auxotroph. However, despite encoding asparaginyl-tRNA synthetase and glutaminyl-tRNA synthetase, B. bacteriovorus also contains the amidotransferase GatCAB. Deinococcus radi...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Public Library of Science
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4206432/ https://www.ncbi.nlm.nih.gov/pubmed/25338061 http://dx.doi.org/10.1371/journal.pone.0110842 |
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author | Alperstein, Ariel Ulrich, Brittany Garofalo, Denise M. Dreisbach, Ruth Raff, Hannah Sheppard, Kelly |
author_facet | Alperstein, Ariel Ulrich, Brittany Garofalo, Denise M. Dreisbach, Ruth Raff, Hannah Sheppard, Kelly |
author_sort | Alperstein, Ariel |
collection | PubMed |
description | The predatory bacterium Bdellovibrio bacteriovorus preys on other Gram-negative bacteria and was predicted to be an asparagine auxotroph. However, despite encoding asparaginyl-tRNA synthetase and glutaminyl-tRNA synthetase, B. bacteriovorus also contains the amidotransferase GatCAB. Deinococcus radiodurans, and Thermus thermophilus also encode both of these aminoacyl-tRNA synthetases with GatCAB. Both also code for a second aspartyl-tRNA synthetase and use the additional aspartyl-tRNA synthetase with GatCAB to synthesize asparagine on tRNA(Asn). Unlike those two bacteria, B. bacteriovorus encodes only one aspartyl-tRNA synthetase. Here we demonstrate the lone B. bacteriovorus aspartyl-tRNA synthetase catalyzes aspartyl-tRNA(Asn) formation that GatCAB can then amidate to asparaginyl-tRNA(Asn). This non-discriminating aspartyl-tRNA synthetase with GatCAB thus provides B. bacteriovorus a second route for Asn-tRNA(Asn) formation with the asparagine synthesized in a tRNA-dependent manner. Thus, in contrast to a previous prediction, B. bacteriovorus codes for a biosynthetic route for asparagine. Analysis of bacterial genomes suggests a significant number of other bacteria may also code for both routes for Asn-tRNA(Asn) synthesis with only a limited number encoding a second aspartyl-tRNA synthetase. |
format | Online Article Text |
id | pubmed-4206432 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-42064322014-10-27 The Predatory Bacterium Bdellovibrio bacteriovorus Aspartyl-tRNA Synthetase Recognizes tRNA(Asn) as a Substrate Alperstein, Ariel Ulrich, Brittany Garofalo, Denise M. Dreisbach, Ruth Raff, Hannah Sheppard, Kelly PLoS One Research Article The predatory bacterium Bdellovibrio bacteriovorus preys on other Gram-negative bacteria and was predicted to be an asparagine auxotroph. However, despite encoding asparaginyl-tRNA synthetase and glutaminyl-tRNA synthetase, B. bacteriovorus also contains the amidotransferase GatCAB. Deinococcus radiodurans, and Thermus thermophilus also encode both of these aminoacyl-tRNA synthetases with GatCAB. Both also code for a second aspartyl-tRNA synthetase and use the additional aspartyl-tRNA synthetase with GatCAB to synthesize asparagine on tRNA(Asn). Unlike those two bacteria, B. bacteriovorus encodes only one aspartyl-tRNA synthetase. Here we demonstrate the lone B. bacteriovorus aspartyl-tRNA synthetase catalyzes aspartyl-tRNA(Asn) formation that GatCAB can then amidate to asparaginyl-tRNA(Asn). This non-discriminating aspartyl-tRNA synthetase with GatCAB thus provides B. bacteriovorus a second route for Asn-tRNA(Asn) formation with the asparagine synthesized in a tRNA-dependent manner. Thus, in contrast to a previous prediction, B. bacteriovorus codes for a biosynthetic route for asparagine. Analysis of bacterial genomes suggests a significant number of other bacteria may also code for both routes for Asn-tRNA(Asn) synthesis with only a limited number encoding a second aspartyl-tRNA synthetase. Public Library of Science 2014-10-22 /pmc/articles/PMC4206432/ /pubmed/25338061 http://dx.doi.org/10.1371/journal.pone.0110842 Text en © 2014 Alperstein et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Alperstein, Ariel Ulrich, Brittany Garofalo, Denise M. Dreisbach, Ruth Raff, Hannah Sheppard, Kelly The Predatory Bacterium Bdellovibrio bacteriovorus Aspartyl-tRNA Synthetase Recognizes tRNA(Asn) as a Substrate |
title | The Predatory Bacterium Bdellovibrio bacteriovorus Aspartyl-tRNA Synthetase Recognizes tRNA(Asn) as a Substrate |
title_full | The Predatory Bacterium Bdellovibrio bacteriovorus Aspartyl-tRNA Synthetase Recognizes tRNA(Asn) as a Substrate |
title_fullStr | The Predatory Bacterium Bdellovibrio bacteriovorus Aspartyl-tRNA Synthetase Recognizes tRNA(Asn) as a Substrate |
title_full_unstemmed | The Predatory Bacterium Bdellovibrio bacteriovorus Aspartyl-tRNA Synthetase Recognizes tRNA(Asn) as a Substrate |
title_short | The Predatory Bacterium Bdellovibrio bacteriovorus Aspartyl-tRNA Synthetase Recognizes tRNA(Asn) as a Substrate |
title_sort | predatory bacterium bdellovibrio bacteriovorus aspartyl-trna synthetase recognizes trna(asn) as a substrate |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4206432/ https://www.ncbi.nlm.nih.gov/pubmed/25338061 http://dx.doi.org/10.1371/journal.pone.0110842 |
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