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Nucleotide utilization requirements that render ClpB active as a chaperone
Author(s) -
del Castillo Urko,
Fernández-Higuero José Ángel,
Pérez-Acebrón Sergio,
Moro Fernando,
Muga Arturo
Publication year - 2010
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/j.febslet.2010.01.029
Subject(s) - clpb , random hexamer , nucleotide , atp hydrolysis , biochemistry , chaperone (clinical) , protein subunit , chemistry , mutant , biology , enzyme , atpase , gene , medicine , pathology
ClpB is a member of the AAA+ superfamily that forms a ring‐shaped homohexamer. Each protomer contains two nucleotide binding domains arranged in two rings that hydrolyze ATP. We extend here previous studies on ClpB nucleotide utilization requirements by using an experimental approach that maximizes random incorporation of different subunits into the protein hexamer. Incorporation of one subunit unable to bind or hydrolyze ATP knocks down the chaperone activity, while the wt hexamer can accommodate two mutant subunits that hydrolyze ATP in only one protein ring. Four subunits seem to build the functional cooperative unit, provided that one of the protein rings contains active nucleotide binding sites.