期刊
NATURE REVIEWS MICROBIOLOGY
卷 14, 期 1, 页码 33-44出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nrmicro.2015.4
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资金
- US National Institutes of Health (NIH) [AI-16892, GM-101988, GM-49224]
- Howard Hughes Medical Institute
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI016892] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM101988, R01GM049224] Funding Source: NIH RePORTER
To maintain protein homeostasis, AAA+ proteolytic machines degrade damaged and unneeded proteins in bacteria, archaea and eukaryotes. This process involves the ATP-dependent unfolding of a target protein and its subsequent translocation into a self-compartmentalized proteolytic chamber. Related AAA+ enzymes also disaggregate and remodel proteins. Recent structural and biochemical studies, in combination with direct visualization of unfolding and translocation in single-molecule experiments, have illuminated the molecular mechanisms behind these processes and suggest how remodelling of macromolecular complexes by AAA+ enzymes could occur without global denaturation. In this Review, we discuss the structural and mechanistic features of AAA+ proteases and remodelling machines, focusing on the bacterial ClpXP and ClpX as paradigms. We also consider the potential of these enzymes as antibacterial targets and outline future challenges for the field.
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