HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Breton, R. Articles by Lapointe, J. Search for Related Content PubMed PubMed Citation Articles by Breton, R. Articles by Lapointe, J. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 261, Issue 23, 10610-10617, 08, 1986

Glutamyl-tRNA synthetase of Escherichia coli. Isolation and primary structure of the gltX gene and homology with other aminoacyl-tRNA synthetases

R Breton, H Sanfacon, I Papayannopoulos, K Biemann and J Lapointe

The gltX gene encoding the glutamyl-tRNA synthetase of Escherichia coli and adjacent regulatory regions was isolated and sequenced. The structural gene encodes a protein of 471 amino acids whose molecular weight is 53,810. The codon usage is that of genes highly expressed in E. coli. The amino acid sequence deduced from the nucleotide sequence of the gltX gene was confirmed by mass spectrometry of large peptides derived from the glutamyl-tRNA synthetase. The observed peptides confirm 73% of the predicted sequence, including the NH2-terminal and the COOH-terminal segments. Sequence homology between the glutamyl-tRNA synthetase and other aminoacyl-tRNA synthetases of E. coli was found in four segments. Three of them are aligned in the same order in all the synthetases where they are present, but the intersegment spacings are not constant; these ordered segments may come from a progenitor to which other domains were added. Starting from the NH2-end, the first two segments are part of a longer region of homology with the glutaminyl-tRNA synthetase, without need for gaps; its size, about 100 amino acids, is typical of a single folding domain. In the first segment, containing sequences homologous to the HIGH consensus, the homology is consistent with the following evolutionary linkage: gltX---- glnS----metS----ileS and tyrS.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				M. K. B. Berlyn Linkage Map of Escherichia coli K-12, Edition 10: The Traditional Map Microbiol. Mol. Biol. Rev., September 1, 1998; 62(3): 814 - 984. [Abstract] [Full Text] [PDF]

				M. Odaert, A. Devalckenaere, P. Trieu-Cuot, and M. Simonet Molecular Characterization of IS1541 Insertions in the Genome of Yersinia pestis J. Bacteriol., January 1, 1998; 180(1): 178 - 181. [Abstract] [Full Text]

				Y. Gagnon, L. Lacoste, N. Champagne, and J. Lapointe Widespread Use of the Glu-tRNAGln Transamidation Pathway among Bacteria. A MEMBER OF THE alpha PURPLE BACTERIA LACKS GLUTAMINYL-tRNA SYNTHETASE J. Biol. Chem., June 21, 1996; 271(25): 14856 - 14863. [Abstract] [Full Text] [PDF]

				O Nureki, D. Vassylyev, K Katayanagi, T Shimizu, S Sekine, T Kigawa, T Miyazawa, S Yokoyama, and K Morikawa Architectures of class-defining and specific domains of glutamyl-tRNA synthetase Science, March 31, 1995; 267(5206): 1958 - 1965. [Abstract] [PDF]