NDLI: The GroE chaperonin machine is the major modulator of the CIRCE heat shock regulon ofBacillus subtilis

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Journal of Biosciences : Volume 23, Issue 3, September 1998

Journal of Biosciences : Volume 23, Issue 2, June 1998

Journal of Biosciences : Volume 23, Issue 1, March 1998

Journal of Biosciences : Volume 22

The GroE chaperonin machine is the major modulator of the CIRCE heat shock regulon ofBacillus subtilis

Content Provider	Springer Nature Link
Author	Schumann, Wolfgang Homuth, Georg Mogk, Axel
Copyright Year	1998
Abstract	Regulation of the heat shock response in bacteria has been studied extensively inEscherichia coli where heat shock genes are classified into three classes and where each class is regulated by a different alternate sigma factor.Bacillus subtilis serves as a second model bacterium to study regulation of the heat shock response in detail. Here, four classes of heat shock genes have been described so far where two are controlled by two different repressor proteins and the third by the alternate sigma factorσ $^{ B }$. Class I heat shock genes consists of two operons, the heptacistronicdnaK and the bicistronicgroE operon. Transcription of thednaK operon is complex involving two promoters, premature termination of transcription, mRNA processing and different stabilities of the processed transcripts to ensure the appropriate amounts of heat shock proteins under different growth conditions. The translation product of thehrcA gene, the first gene of thednaK operon, binds to an operator designated CIRCE element, and its activity is modulated by the GroE chaperonin system. We assume that the HrcA protein, uponde novo synthesis and upon dissociation from its operator, is present in an inactive form and has to be activated by the GroE chaperonin system resulting in an HrcA-GroE reaction cycle. Induction of class I heat shock genes occurs by the appearance of denatured proteins within the cytoplasm which titrate the GroE system. This results in accumulation of inactive HrcA repressor and thereby in induction of class I heat shock genes. Upon removal of the non-native proteins from the cytoplasm, the GroE chaperonin will interact with HrcA and promote folding into its active conformation resulting in turning off of class I heat shock genes. This mechanism ensures adequate adjustment of class I heat shock proteins depending on their actual need.
Starting Page	415
Ending Page	422
Page Count	8
File Format	PDF
ISSN	02505991
Journal	Journal of Biosciences
Volume Number	23
Issue Number	4
e-ISSN	09737138
Language	English
Publisher	Springer India
Publisher Date	1998-01-01
Publisher Institution	Indian Academy of Sciences
Publisher Place	New Delhi
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Heat shock response CIRCE HrcA GroEL DnaK repressor Life Sciences Biomedicine general Zoology Plant Sciences Microbiology Cell Biology
Content Type	Text
Resource Type	Article
Subject	Medicine Biochemistry, Genetics and Molecular Biology Agricultural and Biological Sciences

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The GroE chaperonin machine is the major modulator of the CIRCE heat shock regulon ofBacillus subtilis

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The GroE chaperonin machine is the major modulator of the CIRCE heat shock regulon ofBacillus subtilis