Binding of MG132 or Deletion of the Thr Active Sites in HslV Subunits Increases the Affinity of HslV Protease for HslU ATPase and Makes This Interaction Nucleotide-independent

HslVU is an ATP-dependent protease in bacteria consisting of HslV dodecamer and HslU hexamer. Upon ATP binding, HslU ATPase allosterically activates the catalytic function of HslV protease by 1–2 orders of magnitude. However, relatively little is known about the role of HslV in the control of HslU f...

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Bibliographic Details
Main Authors: Park, Eunyong, Lee, Jung Wook, Eom, Soo Hyun, Seol, Jae Hong, Chung, Chin Ha
Format: Artigo
Language:Inglês
Published: American Society for Biochemistry and Molecular Biology 2008
Subjects:
Enzyme Catalysis and Regulation
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC2662256/
https://ncbi.nlm.nih.gov/pubmed/18838376
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M805411200
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