Affiliation:
1. Institut de Biologie Moléculaire et d'Ingénierie Génétique, ESA CNRS 6031, Université de Poitiers, 86022 Poitiers Cedex, France
Abstract
ABSTRACT
We have isolated the structural gene for translation initiation factor IF2 (
infB
) from the myxobacterium
Myxococcus xanthus
. The gene (3.22 kb) encodes a 1,070-residue protein showing extensive homology within its G domain and C terminus to the equivalent regions of IF2 from
Escherichia coli
. The protein cross-reacts with antibodies raised against
E. coli
IF2 and was able to complement an
E. coli infB
mutant. The
M. xanthus
protein is the largest IF2 known to date. This is essentially due to a longer N-terminal region made up of two characteristic domains. The first comprises a 188-amino-acid sequence consisting essentially of alanine, proline, valine, and glutamic acid residues, similar to the APE domain observed in
Stigmatella aurantiaca
IF2. The second is unique to
M. xanthus
IF2, is located between the APE sequence and the GTP binding domain, and consists exclusively of glycine, proline, and arginine residues.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
2 articles.
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