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The predatory bacterium Bdellovibrio bacteriovorus aspartyl-tRNA synthetase recognizes tRNAAsn as a substrate.
Alperstein, Ariel; Ulrich, Brittany; Garofalo, Denise M; Dreisbach, Ruth; Raff, Hannah; Sheppard, Kelly.
Afiliación
  • Alperstein A; Chemistry Department, Skidmore College, Saratoga Springs, New York, United States of America.
  • Ulrich B; Chemistry Department, Skidmore College, Saratoga Springs, New York, United States of America.
  • Garofalo DM; Chemistry Department, Skidmore College, Saratoga Springs, New York, United States of America.
  • Dreisbach R; Chemistry Department, Skidmore College, Saratoga Springs, New York, United States of America.
  • Raff H; Chemistry Department, Skidmore College, Saratoga Springs, New York, United States of America.
  • Sheppard K; Chemistry Department, Skidmore College, Saratoga Springs, New York, United States of America.
PLoS One ; 9(10): e110842, 2014.
Article en En | MEDLINE | ID: mdl-25338061
ABSTRACT
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 tRNAAsn. Unlike those two bacteria, B. bacteriovorus encodes only one aspartyl-tRNA synthetase. Here we demonstrate the lone B. bacteriovorus aspartyl-tRNA synthetase catalyzes aspartyl-tRNAAsn formation that GatCAB can then amidate to asparaginyl-tRNAAsn. This non-discriminating aspartyl-tRNA synthetase with GatCAB thus provides B. bacteriovorus a second route for Asn-tRNAAsn 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-tRNAAsn synthesis with only a limited number encoding a second aspartyl-tRNA synthetase.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Aspartato-ARNt Ligasa / Proteínas Bacterianas / Bdellovibrio / ARN de Transferencia de Asparagina Idioma: En Revista: PLoS One Asunto de la revista: CIENCIA / MEDICINA Año: 2014 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Aspartato-ARNt Ligasa / Proteínas Bacterianas / Bdellovibrio / ARN de Transferencia de Asparagina Idioma: En Revista: PLoS One Asunto de la revista: CIENCIA / MEDICINA Año: 2014 Tipo del documento: Article País de afiliación: Estados Unidos
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