Nucleotide utilization requirements that render ClpB active as a chaperone.
FEBS Lett
; 584(5): 929-34, 2010 Mar 05.
Article
en En
| MEDLINE
| ID: mdl-20085762
ABSTRACT
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Chaperonas Moleculares
/
Proteínas de Escherichia coli
/
Proteínas de Choque Térmico
/
Nucleótidos
Idioma:
En
Revista:
FEBS Lett
Año:
2010
Tipo del documento:
Article
País de afiliación:
España