Document Detail

Efficient export of alkaline phosphatase overexpressed from a multicopy plasmid requires degP, a gene encoding a periplasmic protease of Escherichia coli.
MedLine Citation:
PMID:  12483555     Owner:  NLM     Status:  Publisher    
Escherichia coli DegP is an inducible serine protease which is involved in the breakdown of abberant proteins arising in the periplasmic compartment. Overexpression of alkaline phosphatase (PhoA) increased transcription of degP by twofold. To examine the significance of its induction, we overexpressed PhoA in a mutant strain deficient in the degP gene. Upon PhoA overexpression, the degP mutant produced a smaller amount of active PhoA, about one half of the enzymatic activity of its isogenic wild-type strain, and accumulated a larger amount of its precursor, indicating that degP is required for efficient export of overexpressed PhoA. Pulse-chase experiment showed that PhoA overexpression in the absence of degP causes a severe defect in the export of several proteins tested. Examination of the synthesis and the accumulation of the phoA gene products revealed that a part of them, synthesized in the wild-type strain, undergoes relatively rapid proteolysis and that degP is necessary for such a process. From these results, we discuss a possible role of DegP in facilitating protein export under stress conditions.
Hiroshi Kadokura; Hiroyuki Kawasaki; Koji Yoda; Makari Yamasaki; Katsuhiko Kitamoto
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Publication Detail:
Journal Detail:
Title:  The Journal of general and applied microbiology     Volume:  47     ISSN:  0022-1260     ISO Abbreviation:  J. Gen. Appl. Microbiol.     Publication Date:  2001 Jun 
Date Detail:
Created Date:  2002-Dec-16     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0165543     Medline TA:  J Gen Appl Microbiol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  133-141     Citation Subset:  -    
Department of Biotechnology, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan.
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