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J. Bacteriol., Sep 1995, 4851-4856, Vol 177, No. 17
JA Maupin-Furlow, JK Rosentel, JH Lee, U Deppenmeier, RP Gunsalus and KT Shanmugam
DNA sequence analysis of the modABCD operon of Escherichia coli revealed
the presence of four open reading frames. The first gene, modA, codes for a
257-amino-acid periplasmic binding protein enunciated by the presence of a
signal peptide-like sequence. The second gene (modB) encodes a
229-amino-acid protein with a potential membrane location, while the
352-amino-acid ModC protein (modC product) contains a nucleotide-binding
motif. On the basis of sequence similarities with proteins from other
transport systems and molybdate transport proteins from other organisms,
these three proteins are proposed to constitute the molybdate transport
system. The fourth open reading frame (modD) encodes a 231-amino-acid
protein of unknown function. Plasmids containing different mod genes were
used to map several molybdate- suppressible chlorate-resistant mutants;
interestingly, none of the 40 mutants tested had a mutation in the modD
gene. About 35% of these chlorate-resistant mutants were not complemented
by mod operon DNA. These mutants, designated mol, contained mutations at
unknown chromosomal location(s) and produced formate hydrogenlyase activity
only when cultured in molybdate-supplemented glucose-minimal medium, not in
L broth. This group of mol mutants constitutes a new class of molybdate
utilization mutants distinct from other known mutants in molybdate
metabolism. These results show that molybdate, after transport into cells
by the ModABC proteins, is metabolized (activated?) by the products of the
mol gene(s).
Copyright © 1995, American Society for Microbiology
Genetic analysis of the modABCD (molybdate transport) operon of Escherichia coli
Department of Microbiology and Cell Science, University of Florida, Gainesville 32611, USA.
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