Thiobacillus ferrooxidans tyrosyl-tRNA synthetase functions in vivo in Escherichia coli
Author
dc.contributor.author
Salazar, G.
Author
dc.contributor.author
Sagredo,
Author
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Jedlicki,
Author
dc.contributor.author
Soll,
Author
dc.contributor.author
Weygand-Durasevic,
Author
dc.contributor.author
Orellana,
Admission date
dc.date.accessioned
2019-01-29T15:49:56Z
Available date
dc.date.available
2019-01-29T15:49:56Z
Publication date
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1994
Cita de ítem
dc.identifier.citation
Journal of Bacteriology, Volumen 176, Issue 14, 2018, Pages 4409-4415
Identifier
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00219193
Identifier
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10.1128/jb.176.14.4409-4415.1994
Identifier
dc.identifier.uri
https://repositorio.uchile.cl/handle/2250/162491
Abstract
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The tyrosyl-tRNA synthetase gene (tyrZ) from Thiobacillus ferrooxidans, an acidophilic, autotrophic, gram-negative bacterium that participates in bioleaching of minerals, was cloned and sequenced. The encoded polypeptide (TyrRZ) is 407 amino acids in length (molecular mass; 38 kDa). The predicted protein sequence has an extensive overall identity (44%) to the sequence of the protein encoded by the Bacillus subtilis tyrZ gene, one of the two genes encoding tyrosyl-tRNA synthetases in this microorganism. Alignment with Escherichia coli TyrRS revealed limited overall identity (24%), except in the regions of the signature sequence for class I aminoacyl-tRNA synthetases. Complementation of an E. coli strain with a thermosensitive mutation in TyrRS showed that the protein encoded by the T. ferrooxidans tyrZ gene is functional and recognizes the E. coli tRNA(Tyr) as a substrate. TyrZ is a single-copy gene as revealed by Southern blot analysis. The gene was localized upstream from the putative