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Nested cooperativity and salt dependence of the ATPase activity of the archaeal chaperonin Mm‐cpn
Author(s) -
Kusmierczyk Andrew R,
Martin Jörg
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00722-1
Subject(s) - chaperonin , atp hydrolysis , cooperativity , chemistry , hydrolysis , atpase , potassium , gtp' , biochemistry , sodium , salt (chemistry) , biophysics , enzyme , biology , protein folding , organic chemistry
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.