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J Phys Chem B. 2012 Jun 14;116(23):6717-24. doi: 10.1021/jp212024b. Epub 2012 Mar 6.

Role of the N-terminal domain of the chaperone ClpX in the recognition and degradation of lambda phage protein O.

Author information

1
Department of Biochemistry, University of Toronto, 1 King's College Circle, Medical Sciences Building, Toronto, Ontario M5S 1A8, Canada.

Abstract

The ClpXP ATPase-protease complex is a key element of the protein quality control machinery in the cell. ClpX consists of a zinc-binding domain (ZBD) that forms dimers and a AAA(+) domain that arranges into a hexamer in an ATP-dependent manner. Here, we report the binding site of the ClpX substrate λ phage protein O (λO) on ZBD(2) in ClpX using NMR and mutagenesis analysis. λO protein was found to interact with a hydrophobic patch on the larger surface of ZBD(2). The affinity of λO toward ZBD(2) was investigated using a quantitative optical biosensor method of dual polarization interferometry. The data suggest overlapping binding sites of λO and the ClpX cofactor SspB on the ZBD(2). Interestingly, a single key mutation in ZBD was found to enhance the ClpXP-dependent degradation of λO.

PMID:
22360725
DOI:
10.1021/jp212024b
[Indexed for MEDLINE]

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