Isolation of the stable hexameric DnaK·DnaJ complex from Thermus thermophilus
作者： K Motohashi , H Taguchi , N Ishii , M Yoshida
DOI: 10.1016/S0021-9258(18)47127-X
关键词: Mole 、 Thermus thermophilus 、 Crystallography 、 Atpase activity 、 Gene 、 Bacteria 、 Ring (chemistry) 、 Molecule 、 Thermophile 、 Biology
摘要: A DnaK homolog (T.DnaK) has been purified as a stable complex with DnaJ (T.DnaJ) from thermophilic bacterium, Thermus thermophilus. This an approximate molecular size of 300 kDa and appears to contain three copies each T.DnaK T.DnaJ molecules. Consistently, trigonal ring structures diameter (trigonal apex-to-apex) about 11 nm were observed electron microscopy. The no endogenously bound AT(D)P is in the presence Mg-AT(D)P. It possesses weak ATPase activity retains 3 mol ADP/mole when incubated Mg-ATP. able interact reduced carboxymethylated alpha-lactalbumin which we used model unfolded protein.
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