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[Au] Autor:Bittner LM; Arends J; Narberhaus F
[Ad] Endereço:Microbial Biology, Ruhr University Bochum, Bochum, Germany.
[Ti] Título:Mini review: ATP-dependent proteases in bacteria.
[So] Source:Biopolymers;105(8):505-17, 2016 Aug.
[Is] ISSN:1097-0282
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:AAA(+) proteases are universal barrel-like and ATP-fueled machines preventing the accumulation of aberrant proteins and regulating the proteome according to the cellular demand. They are characterized by two separate operating units, the ATPase and peptidase domains. ATP-dependent unfolding and translocation of a substrate into the proteolytic chamber is followed by ATP-independent degradation. This review addresses the structure and function of bacterial AAA(+) proteases with a focus on the ATP-driven mechanisms and the coordinated movements in the complex mainly based on the knowledge of ClpXP. We conclude by discussing strategies how novel protease substrates can be trapped by mutated AAA(+) protease variants. © 2016 Wiley Periodicals, Inc. Biopolymers 105: 505-517, 2016.
[Mh] Termos MeSH primário: Endopeptidases Dependentes de ATP/metabolismo
Trifosfato de Adenosina/metabolismo
Proteínas de Bactérias/metabolismo
[Mh] Termos MeSH secundário: Endopeptidases Dependentes de ATP/química
Trifosfato de Adenosina/química
Proteínas de Bactérias/química
Especificidade por Substrato/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (ATP-Dependent Endopeptidases); 0 (Bacterial Proteins); 8L70Q75FXE (Adenosine Triphosphate)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170206
[Lr] Data última revisão:
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160315
[St] Status:MEDLINE
[do] DOI:10.1002/bip.22831

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[Au] Autor:Bartoszewska M; Williams C; Kikhney A; Opalinski L; van Roermund CW; de Boer R; Veenhuis M; van der Klei IJ
[Ad] Endereço:Molecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, Kluyver Centre for Genomics of Industrial Fermentation, P. O. Box 11103, 9700CC Groningen, The Netherlands.
[Ti] Título:Peroxisomal proteostasis involves a Lon family protein that functions as protease and chaperone.
[So] Source:J Biol Chem;287(33):27380-95, 2012 Aug 10.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proteins are subject to continuous quality control for optimal proteostasis. The knowledge of peroxisome quality control systems is still in its infancy. Here we show that peroxisomes contain a member of the Lon family of proteases (Pln). We show that Pln is a heptameric protein and acts as an ATP-fueled protease and chaperone. Hence, Pln is the first chaperone identified in fungal peroxisomes. In cells of a PLN deletion strain peroxisomes contain protein aggregates, a major component of which is catalase-peroxidase. We show that this enzyme is sensitive to oxidative damage. The oxidatively damaged, but not the native protein, is a substrate of the Pln protease. Cells of the pln strain contain enhanced levels of catalase-peroxidase protein but reduced catalase-peroxidase enzyme activities. Together with the observation that Pln has chaperone activity in vitro, our data suggest that catalase-peroxidase aggregates accumulate in peroxisomes of pln cells due to the combined absence of Pln protease and chaperone activities.
[Mh] Termos MeSH primário: Endopeptidases Dependentes de ATP/metabolismo
Proteínas Fúngicas/metabolismo
Chaperonas Moleculares/metabolismo
Penicillium chrysogenum/enzimologia
[Mh] Termos MeSH secundário: Endopeptidases Dependentes de ATP/genética
Proteínas Fúngicas/genética
Chaperonas Moleculares/genética
Estresse Oxidativo/fisiologia
Penicillium chrysogenum/genética
[Nm] Nome de substância:
0 (ATP-Dependent Endopeptidases); 0 (Fungal Proteins); 0 (Molecular Chaperones); EC (Catalase)
[Em] Mês de entrada:1211
[Cu] Atualização por classe:150224
[Lr] Data última revisão:
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120627
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M112.381566

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