title: Mini review: ATP-dependent proteases in bacteria.
abstract: 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.
authors.affiliation: Microbial Biology, Ruhr University Bochum, Bochum, Germany.
authors.forename: Lisa-Marie
authors.initials: LM
authors.lastname: Bittner
authors.affiliation: Microbial Biology, Ruhr University Bochum, Bochum, Germany.
authors.forename: Jan
authors.initials: J
authors.lastname: Arends
authors.affiliation: Microbial Biology, Ruhr University Bochum, Bochum, Germany.
authors.forename: Franz
authors.initials: F
authors.lastname: Narberhaus
mesh_terms: D057065:ATP-Dependent Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism*; D001419:Bacteria / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity / Q000502:physiology
chemical_list: D057065:ATP-Dependent Endopeptidases; D001426:Bacterial Proteins; D000255:Adenosine Triphosphate
keywords: AAA protein; ATPase; protease