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J Bacteriol, March 1998, p. 1174-1184, Vol. 180, No. 5
Department of Microbiology and Immunology,
Loyola University Chicago Stritch School of Medicine, Maywood,
Illinois 60153
Received 23 September 1997/Accepted 16 December 1997
Complex I (EC 1.6.99.3) of the bacterium Escherichia
coli is considered to be the minimal form of the type I NADH
dehydrogenase, the first enzyme complex in the respiratory chain.
Because of its small size and relative simplicity, the E. coli enzyme has become a model used to identify and characterize
the mechanism(s) by which cells regulate the synthesis and assembly of
this large respiratory complex. To begin dissecting the processes by
which E. coli cells regulate the expression of
nuo and the assembly of complex I, we undertook a genetic
analysis of the nuo locus, which encodes the 14 Nuo
subunits comprising E. coli complex I. Here we present the
results of studies, performed on an isogenic collection of
nuo mutants, that focus on the physiological, biochemical, and molecular consequences caused by the lack of or defects in several
Nuo subunits. In particular, we present evidence that NuoG, a
peripheral subunit, is essential for complex I function and that it
plays a role in the regulation of nuo expression and/or the
assembly of complex I.
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Genetic Analysis of the nuo Locus, Which
Encodes the Proton-Translocating NADH Dehydrogenase in
Escherichia coli
and
*
Corresponding author. Mailing address: Department of
Microbiology and Immunology, Loyola University Chicago Stritch School of Medicine, 2160 S. First Ave., Building 105, Room 3822, Maywood, IL
60153. Phone: (708) 216-5814. Fax: (708) 216-9574. E-mail: awolfe{at}luc.edu.
Present address: University of Illinois at Chicago, Department of
Medicine/Digestive and Liver Disease, Chicago, IL 60612.
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