Literature DB >> 12359246

The beta subunit of Aquifex aeolicus leucyl-tRNA synthetase is responsible for cognate tRNA recognition.

Masaki Gouda1, Takashi Yokogawa, Kazuya Nishikawa.   

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.

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Year:  2002        PMID: 12359246     DOI: 10.1016/s0006-291x(02)02281-7

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  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.

Authors:  Yong-Gang Zheng; Hui Wei; Chen Ling; Franck Martin; Gilbert Eriani; En-Duo Wang
Journal:  Nucleic Acids Res       Date:  2004-06-18       Impact factor: 16.971

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

Authors:  Dagmar K Willkomm; Jens Minnerup; Alexander Hüttenhofer; Roland K Hartmann
Journal:  Nucleic Acids Res       Date:  2005-04-06       Impact factor: 16.971

  2 in total

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