<b>The Clp ATPases define a novel class of molecular chaperones</b>

Wawrzynów, Alicja; Banecki, Bogdan; Żylicz, Maciej

doi:10.1046/j.1365-2958.1996.421404.x

Cited by 123 publications

(94 citation statements)

References 18 publications

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“…Like ClpB, many of the ATPases also display chaperone activities (e.g. protein unfolding/refolding) independently of their roles in proteolysis (Wawrzynow et al ., 1996).…”

Section: Clppmentioning

confidence: 99%

Self‐compartmentalized bacterial proteases and pathogenesis

Butler

Festa

Pearce

et al. 2006

Molecular Microbiology

107

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SummaryProtein degradation is required for homeostasis of all living organisms. Self-compartmentalized ATPdependent proteases are required for virulence of several pathogenic bacteria. Among the proteases implicated are ClpP and Lon, as well as the more recently identified bacterial proteasome. It is generally assumed that when a pathogen invades a host, microbial proteins become irreversibly damaged and need to be degraded. However, recent data suggest that proteolysis is also essential for virulence gene regulation. In this review, we will discuss what is known about the relationship between ATP-dependent proteolysis and pathogenesis. In addition, we will propose other potential roles these chambered proteases may have in bacterial virulence. Importantly, these proteases show promise as targets for antimicrobial therapy.

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“…Like ClpB, many of the ATPases also display chaperone activities (e.g. protein unfolding/refolding) independently of their roles in proteolysis (Wawrzynow et al ., 1996).…”

Section: Clppmentioning

confidence: 99%

Self‐compartmentalized bacterial proteases and pathogenesis

Butler

Festa

Pearce

et al. 2006

Molecular Microbiology

107

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“…Expression of the sip genes appeared to be coordinated by complex regulatory signals, including the pleiotropic transcriptional activator PrfA, and stress proteins involved in L. monocytogenes pathogenicity. Clp ATPases are believed to form part of post-translation regulatory networks that ensure survival in stress conditions, presumably by acting as molecular chaperones that mediate the repair or scavenging of damaged proteins (Wawrzynow et al, 1996). In B. subtilis, Clp ATPases mediate adaptive responses to stress conditions, as well as to many other different processes, including the development of competence, sporulation, exoenzyme synthesis and cell-cycle regulation.…”

Section: Regulation Of Spase I Expression In Infected Cellsmentioning

confidence: 99%

Regulation of expression of type I signal peptidases in Listeria monocytogenes

Raynaud

Charbit

2005

Microbiology

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The role of type I signal peptidases (SPases I) is to remove the signal peptides of preproteins exported by the general secretory pathway. The genome of Listeria monocytogenes contains a locus encoding three contiguous SPases I (denoted SipX, SipY and SipZ). The authors recently showed that SipX and SipZ perform distinct functions in protein secretion and bacterial pathogenicity. Here, the regulation of sip gene expression in broth and in infected eukaryotic cells was studied. The results show that expression of the three sip genes is (i) controlled by two distinct promoter regions that respond differently to growth phase and temperature variations, and (ii) influenced by PrfA (the transcriptional activator regulating most of the virulence genes of L. monocytogenes) and the stress proteins ClpC and ClpP. It was found that sip gene expression was strongly upregulated upon infection of eukaryotic cells when bacteria were still entrapped in the phagosomal compartment. This upregulation is compatible with the need of L. monocytogenes to optimize its production of virulence factors in the early stage of the intracellular cycle.

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“…All prokaryotic and eukaryotic organisms express several chaperone proteins of the Clp/Hsp100 family (1,2). Members of this chaperone family were first described in Escherichia coli as ATP-dependent partner proteins of the serine-type protease ClpP.…”

mentioning

confidence: 99%

The ClpB Homolog Hsp78 Is Required for the Efficient Degradation of Proteins in the Mitochondrial Matrix

Röttgers

Zufall²,

Guiard

et al. 2002

Journal of Biological Chemistry

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Molecular chaperones perform vital functions in mitochondrial protein import and folding. In yeast mitochondria, two members of the Clp/Hsp100 chaperone family, Hsp78 and Mcx1, have been identified as homologs of the bacterial proteins ClpB and ClpX, respectively. In this report we employed a novel quantitative assay system to assess the role of Hsp78 and Mcx1 in protein degradation within the matrix. Mitochondria were preloaded with large amounts of two purified recombinant reporter proteins exhibiting different folding stabilities. Proteolysis of the imported substrate proteins depended on the mitochondrial level of ATP and was mediated by the matrix protease Pim1/LON. Degradation rates were found to be independent of the folding stability of the reporter proteins. Mitochondria from hsp78⌬ cells exhibited a significant defect in the degradation efficiency of both substrates even at low temperature whereas mcx1⌬ mitochondria showed wild-type activity. The proteolysis defect in hsp78⌬ mitochondria was independent from the aggregation behavior of the substrate proteins. We conclude that Hsp78 is a genuine component of the mitochondrial proteolysis system required for the efficient degradation of substrate proteins in the matrix.

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The Clp ATPases define a novel class of molecular chaperones

Cited by 123 publications

References 18 publications

Self‐compartmentalized bacterial proteases and pathogenesis

Self‐compartmentalized bacterial proteases and pathogenesis

Regulation of expression of type I signal peptidases in Listeria monocytogenes

The ClpB Homolog Hsp78 Is Required for the Efficient Degradation of Proteins in the Mitochondrial Matrix

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