Aminoacyl-tRNA formation in the extreme thermophile Thermus thermophilus View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-04

AUTHORS

Liang Feng, Constantinos Stathopoulos, Ivan Ahel, Anusri Mitra, Debra Tumbula-Hansen, Thomas Hartsch, Dieter Söll

ABSTRACT

Thermophilic organisms must be capable of accurate translation at temperatures in which the individual components of the translation machinery and also specific amino acids are particularly sensitive. Thermus thermophilus is a good model organism for studies of thermophilic translation because many of the components in this process have undergone structural and biochemical characterization. We have focused on the pathways of aminoacyl-tRNA synthesis for glutamine, asparagine, proline, and cysteine. We show that the T. thermophilus prolyl-tRNA synthetase (ProRS) exhibits cysteinyl-tRNA synthetase (CysRS) activity although the organism also encodes a canonical CysRS. The ProRS requires tRNA for cysteine activation, as is known for the characterized archaeal prolyl-cysteinyl-tRNA synthetase (ProCysRS) enzymes. The heterotrimeric T. thermophilus aspartyl-tRNA(Asn) amidotransferase can form Gln-tRNA in addition to Asn-tRNA: however, a 13-amino-acid C-terminal truncation of the holoenzyme A subunit is deficient in both activities when assayed with homologous substrates. A survey of codon usage in completed prokaryotic genomes identified a higher Glu:Gln ratio in proteins of thermophiles compared to mesophiles. More... »

PAGES

167-174

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s007920100245

DOI

http://dx.doi.org/10.1007/s007920100245

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1028228258

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/12013438


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165 schema:name Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA
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