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Journal of Bacteriology, October 2000, p. 5592-5595, Vol. 182, No. 19
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

Shameema Sarker,1 Kenneth E. Rudd,2 and Donald Oliver1,*

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.

* 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.

Journal of Bacteriology, October 2000, p. 5592-5595, Vol. 182, No. 19
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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