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J Inorg Biochem. 2015 Aug;149:1-5. doi: 10.1016/j.jinorgbio.2015.03.012. Epub 2015 Mar 31.

Metals in the active site of native protein phosphatase-1.

Author information

1
Laboratory of Biosignaling and Therapeutics, Department of Cellular and Molecular Medicine, KU Leuven, Belgium; Department of Chemistry, KU Leuven, Belgium.
2
Interuniversity Micro Electronics Center (IMEC), Leuven, Belgium.
3
Laboratory of Biosignaling and Therapeutics, Department of Cellular and Molecular Medicine, KU Leuven, Belgium.
4
Department of Chemistry, KU Leuven, Belgium.
5
Department of Chemistry, KU Leuven, Belgium; Interuniversity Micro Electronics Center (IMEC), Leuven, Belgium.
6
Laboratory of Biosignaling and Therapeutics, Department of Cellular and Molecular Medicine, KU Leuven, Belgium. Electronic address: Mathieu.Bollen@med.kuleuven.be.

Abstract

Protein phosphatase-1 (PP1) is a major protein Ser/Thr phosphatase in eukaryotic cells. Its activity depends on two metal ions in the catalytic site, which were identified as manganese in the bacterially expressed phosphatase. However, the identity of the metal ions in native PP1 is unknown. In this study, total reflection X-ray fluorescence (TXRF) was used to detect iron and zinc in PP1 that was purified from rabbit skeletal muscle. Metal exchange experiments confirmed that the distinct substrate specificity of recombinant and native PP1 is determined by the nature of their associated metals. We also found that the iron level associated with native PP1 is decreased by incubation with inhibitor-2, consistent with a function of inhibitor-2 as a PP1 chaperone.

KEYWORDS:

Inhibitor-2; Iron; Protein phosphatase-1; TXRF; Zinc

PMID:
25890482
DOI:
10.1016/j.jinorgbio.2015.03.012
[Indexed for MEDLINE]

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