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Properties of the chaperonin complex from the halophilic archaeon Haloferax volcanii
Author(s) -
Large Andrew T,
Kovacs Eszter,
Lund Peter A
Publication year - 2002
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(02)03685-2
Subject(s) - haloferax volcanii , halophile , chaperonin , chemistry , biochemistry , molecular mass , sodium , chromatography , archaea , bacteria , gene , biology , organic chemistry , enzyme , genetics
The halophilic archaeon Haloferax volcanii has three genes encoding type II chaperonins, named cct1 , cct2 and cct3 . We show here that the three CCT proteins are all expressed but not to the same level. All three proteins are further induced on heat shock. The CCT proteins were purified by ammonium sulphate precipitation, sucrose gradient centrifugation and hydrophobic interaction chromatography. This procedure yields a high molecular mass complex (or complexes). The complex has ATPase activity, which is magnesium dependent, low salt‐sensitive and stable to at least 75°C. Activity requires high levels of potassium ions and was reduced in the presence of an increasing concentration of sodium ions.