Metabolic Instability of Escherichia coli Cyclopropane Fatty Acid Synthase Is Due to RpoH-Dependent Proteolysis

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Published inJournal of Bacteriology Vol. 182; no. 15; pp. 4288 - 4294
Main Authors Chang, Y Y, Eichel, J, Cronan, Jr, J E
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.08.2000
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Abstract Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JB .asm.org, visit: JB       
AbstractList Cyclopropane fatty acids (CFAs) are generally synthesized as bacterial cultures enter stationary phase. In Escherichia coli, the onset of CFA synthesis results from increased transcription of cfa, the gene encoding CFA synthase. However, the increased level of CFA synthase activity is transient; the activity quickly declines to the basal level. We report that the loss of CFA activity is due to proteolytic degradation dependent on expression of the heat shock regulon. CFA synthase degradation is unaffected by mutations in the lon, clpP, and groEL genes or by depletion of the intracellular ATP pools. It seems likely that CFA synthase is the target of an unidentified energy-independent heat shock regulon protease. This seems to be the first example of heat shock-dependent degradation of a normal biosynthetic enzyme.
ABSTRACT Cyclopropane fatty acids (CFAs) are generally synthesized as bacterial cultures enter stationary phase. In Escherichia coli , the onset of CFA synthesis results from increased transcription of cfa , the gene encoding CFA synthase. However, the increased level of CFA synthase activity is transient; the activity quickly declines to the basal level. We report that the loss of CFA activity is due to proteolytic degradation dependent on expression of the heat shock regulon. CFA synthase degradation is unaffected by mutations in the lon , clpP , and groEL genes or by depletion of the intracellular ATP pools. It seems likely that CFA synthase is the target of an unidentified energy-independent heat shock regulon protease. This seems to be the first example of heat shock-dependent degradation of a normal biosynthetic enzyme.
Cyclopropane fatty acids (CFAs) are generally synthesized as bacterial cultures enter stationary phase. In Escherichia coli , the onset of CFA synthesis results from increased transcription of cfa , the gene encoding CFA synthase. However, the increased level of CFA synthase activity is transient; the activity quickly declines to the basal level. We report that the loss of CFA activity is due to proteolytic degradation dependent on expression of the heat shock regulon. CFA synthase degradation is unaffected by mutations in the lon , clpP , and groEL genes or by depletion of the intracellular ATP pools. It seems likely that CFA synthase is the target of an unidentified energy-independent heat shock regulon protease. This seems to be the first example of heat shock-dependent degradation of a normal biosynthetic enzyme.
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Cyclopropane fatty acids (CFAs) are generally synthesized as bacterial cultures enter stationary phase. In Escherichia coli, the onset of CFA synthesis results from increased transcription of cfa, the gene encoding CFA synthase.
Author Ying-Ying Chang
John E. Cronan Jr
Johannes Eichel
AuthorAffiliation Departments of Microbiology 1 and Biochemistry, 3 University of Illinois, Urbana, Illinois 61801, and Hans-Knöll Institute for Natural Products Research, 07745 Jena, Germany 2
AuthorAffiliation_xml – name: Departments of Microbiology 1 and Biochemistry, 3 University of Illinois, Urbana, Illinois 61801, and Hans-Knöll Institute for Natural Products Research, 07745 Jena, Germany 2
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Corresponding author. Mailing address: B103 Chemical and Life Sciences Laboratory, 601 South Goodwin Ave., Urbana, IL 61801. Phone: (217) 333-0425. Fax: (217) 244-6697. E-mail: j-cronan@life.uiuc.edu.
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  doi: 10.1016/0022-2836(86)90385-2
– volume: 348
  start-page: 63
  year: 1974
  ident: e_1_3_2_4_2
  article-title: Studies on the biosynthesis of cyclopropane fatty acids in Escherichia coli
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/0005-2760(74)90093-9
  contributor:
    fullname: Cronan J. E.
– volume: 81
  start-page: 6779
  year: 1984
  ident: e_1_3_2_2_2
  article-title: A gene regulating the heat shock response in Escherichia coli also affects proteolysis
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.81.21.6779
  contributor:
    fullname: Baker T. A.
SSID ssj0014452
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Cyclopropane fatty acids (CFAs) are generally synthesized as bacterial cultures enter stationary phase. In Escherichia coli, the onset of CFA synthesis results...
ABSTRACT Cyclopropane fatty acids (CFAs) are generally synthesized as bacterial cultures enter stationary phase. In Escherichia coli , the onset of CFA...
Cyclopropane fatty acids (CFAs) are generally synthesized as bacterial cultures enter stationary phase. In Escherichia coli , the onset of CFA synthesis...
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StartPage 4288
SubjectTerms Adenosine Triphosphatases - genetics
Bacteria
Bacteriology
Biochemistry
CFA synthase
Chaperonin 60 - genetics
Cyclopropane fatty acids
Electrophoresis, Polyacrylamide Gel
Endopeptidase Clp
Enzyme Stability
Enzymes
Escherichia coli
Escherichia coli - enzymology
Fatty acids
Heat-Shock Proteins - metabolism
Metabolism
Methyltransferases - metabolism
Microbiology
Mutagenesis, Site-Directed
Physiology and Metabolism
Regulon - genetics
RpoH protein
Serine Endopeptidases - genetics
Sigma Factor
Time Factors
Transcription Factors - metabolism
Title Metabolic Instability of Escherichia coli Cyclopropane Fatty Acid Synthase Is Due to RpoH-Dependent Proteolysis
URI http://jb.asm.org/content/182/15/4288.abstract
https://www.ncbi.nlm.nih.gov/pubmed/10894739
https://www.proquest.com/docview/227085717/abstract/
https://search.proquest.com/docview/17598193
https://pubmed.ncbi.nlm.nih.gov/PMC101943
Volume 182
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