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The Beta Subunit of Aquifex Aeolicus Leucyl-tRNA Synthetase is Responsible for Cognate TRNA Recognition

Overview
Publisher Elsevier
Specialty Biochemistry
Date 2002 Oct 3
PMID 12359246
Citations 2
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Abstract

The active form of the leucyl-tRNA synthetase from an extreme thermophile Aquifex aeolicus has a heterodimeric (alpha/beta type) quaternary structure that is unique among class I aminoacyl-tRNA synthetases. In an attempt to clarify the individual roles of each subunit in the function of leucyl-tRNA synthetase, several elementary activities were separately measured using each of the subunits alone or the reconstructed alpha/beta complex. It was found that the beta subunit alone is capable of recognizing its cognate tRNA, while the leucyl-adenylate formation and the overall leucyl-tRNA formation are detected only when both of the subunit proteins coexisted.

Citing Articles

Experimental RNomics in Aquifex aeolicus: identification of small non-coding RNAs and the putative 6S RNA homolog.

Willkomm D, Minnerup J, Huttenhofer A, Hartmann R Nucleic Acids Res. 2005; 33(6):1949-60.

PMID: 15814812 PMC: 1074721. DOI: 10.1093/nar/gki334.


Two distinct domains of the beta subunit of Aquifex aeolicus leucyl-tRNA synthetase are involved in tRNA binding as revealed by a three-hybrid selection.

Zheng Y, Wei H, Ling C, Martin F, Eriani G, Wang E Nucleic Acids Res. 2004; 32(11):3294-303.

PMID: 15208367 PMC: 443541. DOI: 10.1093/nar/gkh665.