Cloning and Sequencing of the GltX Gene, Encoding the Glutamyl-tRNA Synthetase of Rhizobium Meliloti A2

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1989 Jul 1

PMID 2661539

Citations 8

Authors

S Laberge

Y Gagnon

L M Bordeleau

J Lapointe

Affiliations

Soon will be listed here.

Abstract

The gltX gene, coding for the glutamyl-tRNA synthetase of Rhizobium meliloti A2, was cloned by using as probe a synthetic oligonucleotide corresponding to the amino acid sequence of a segment of the glutamyl-tRNA synthetase. The codons chosen for this 42-mer were those most frequently used in a set of R. meliloti genes. DNA sequence analysis revealed an open reading frame of 484 codons, encoding a polypeptide of Mr 54,166 containing the amino acid sequences of an NH2-terminal and various internal fragments of the enzyme. Compared with the amino acid sequence of the glutamyl-tRNA synthetase of Escherichia coli, the N-terminal third of the R. meliloti enzyme was strongly conserved (52% identity); the second third was moderately conserved (38% identity) and included a few highly conserved segments, whereas no significant similarity was found in the C-terminal third. These results suggest that the C-terminal part of the protein is probably not involved in the recognition of substrates, a feature shared with other aminoacyl-tRNA synthetases.

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