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Journal of Bacteriology, December 1998, p. 6419-6423, Vol. 180, No. 23
Department of Molecular Biology and
Biochemistry, Wesleyan University, Middletown, Connecticut 06459
Received 11 May 1998/Accepted 5 September 1998
SecA is a dynamic protein that undergoes ATP-dependent membrane
cycling to drive protein translocation across the Escherichia coli inner membrane. To understand more about this process,
azide-resistant (azi) and signal sequence suppressor
(prlD) alleles of secA were studied. We found
that azide resistance is cold sensitive because of a direct effect on
protein export, suggesting that SecA-membrane interaction is regulated
by an endothermic step that is azide inhibitable. secG
function is required for expression of azide-resistant and signal
sequence suppressor activities of azi and prlD
alleles, and in turn, these alleles suppress cold-sensitive and
export-defective phenotypes of a secG null mutant. These
remarkable genetic observations support biochemical data indicating
that SecG promotes SecA membrane cycling and that this process is
dependent on an endothermic change in SecA conformation.
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
secG and Temperature Modulate Expression
of Azide-Resistant and Signal Sequence Suppressor Phenotypes of
Escherichia coli secA Mutants

*
Corresponding author. Mailing address: Department of
Molecular Biology and Biochemistry, Wesleyan University, Middletown, CT
06459. Phone: (860) 685-3556. Fax: (860) 685-2141. E-mail: doliver{at}wesleyan.edu.
Present address: Department of Biochemistry/HHMI, University of
Washington, Seattle, WA 98195.
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