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Journal of Bacteriology, October 2000, p. 5592-5595, Vol. 182, No. 19
Department of Molecular Biology and
Biochemistry, Wesleyan University, Middletown, Connecticut
06459,1 and Department of
Biochemistry and Molecular Biology, University of Miami School of
Medicine, Miami, Florida 331012
Received 30 November 1999/Accepted 6 July 2000
The secretion-responsive regulation of Escherichia coli
secA occurs by coupling its translation to the translation and
secretion of an upstream regulator, secM (formerly geneX).
We revise the translational start site for secM, defining a
new signal peptide sequence with an extended amino-terminal region.
Mutational studies indicate that certain atypical
amino acyl residues within this extended region are critical for proper
secA regulation.
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Revised Translation Start Site for secM Defines an
Atypical Signal Peptide That Regulates Escherichia coli
secA Expression
*
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.
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