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J. Bacteriol., Feb 1996, 1146-1153, Vol 178, No. 4
PR Waller and RT Sauer
The degQ and degS genes of Escherichia coli encode proteins of 455 and 355
residues, respectively, which are homologs of the DegP protease. The
purified DegQ protein has the properties of a serine endoprotease and is
processed by the removal of a 27-residue amino-terminal signal sequence. A
plasmid expressing degQ rescues the temperature-sensitive phenotype of a
strain bearing the degP41 deletion, implying that DegQ, like DegP,
functions as a periplasmic protease in vivo. Deletions in the degQ gene
cause no obvious growth defect, while those in the degS gene result in a
small-colony phenotype. The latter phenotype is rescued by a plasmid
expressing the degS gene but not by plasmids expressing the degQ or degP
genes. This result and the inability of a plasmid expressing degS to rescue
the temperature-sensitive degP41 phenotype indicate that the DegS protein
is functionally different from the DegQ and DegP proteins.
Copyright © 1996, American Society for Microbiology
Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139, USA.
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