Nested cooperativity and salt dependence of the ATPase activity of the archaeal chaperonin Mm-cpn.
- Published Article
Wiley (John Wiley & Sons)
- Publication Date
Jul 17, 2003
The properties of the ATPase activity of the type II chaperonin from Methanococcus maripaludis (Mm-cpn) were examined. Mm-cpn can hydrolyze not only ATP, but also CTP, UTP, and GTP, albeit with different effectiveness. The ATPase activity is dependent on magnesium and potassium ions, and is effectively inhibited by sodium ions. Maximal rates of ATP hydrolysis are achieved at 600 mM potassium. Initial rates of ATP hydrolysis by Mm-cpn were determined at various ATP concentrations, revealing for the first time the presence of both positive intra-ring and negative inter-ring cooperativity in the archaeal chaperonin.
Report this publication
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
This record was last updated on 07/03/2016 and may not reflect the most current and accurate biomedical/scientific data available from NLM.
The corresponding record at NLM can be accessed at https://www.ncbi.nlm.nih.gov/pubmed/12860414