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Characterisation of zinc-binding domains of peroxisomal RING finger proteins using size exclusion chromatography/inductively coupled plasma-mass spectrometry
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Gunda Koellensperger
Published/Copyright:
November 2, 2007
Abstract
We determined the zinc binding stoichiometry of peroxisomal RING finger proteins by measuring sulfur/metal ratios using inductively coupled plasma-mass spectrometry coupled to size exclusion chromatography, a strategy that provides a fast and quantitative overview on the binding of metals in proteins. As a quality control, liquid chromatography-electrospray ionisation-time of flight-mass spectrometry was used to measure the molar masses of the intact proteins. The RING fingers of Pex2p, Pex10p, and Pex12p showed a stoichiometry of 2.0, 2.1, and 1.2 mol zinc/mol protein, respectively. Thus, Pex2p and Pex10p possess a typical RING domain with two coordinated zinc atoms, whereas that of Pex12p coordinates only a single zinc atom.
Keywords: matrix protein import; metal proteins; peroxin; peroxisome biogenesis; PEX2; speciation analysis
Received: 2007-3-15
Accepted: 2007-6-20
Published Online: 2007-11-02
Published in Print: 2007-11-01
©2007 by Walter de Gruyter Berlin New York
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Keywords for this article
matrix protein import;
metal proteins;
peroxin;
peroxisome biogenesis;
PEX2;
speciation analysis
Articles in the same Issue
- Proteinase Inhibitors and Biological Control – An Attractive International Symposia Series
- Two decades of thyroglobulin type-1 domain research
- Cysteine cathepsin non-inhibitory binding partners: modulating intracellular trafficking and function
- Cysteine proteases: destruction ability versus immunomodulation capacity in immune cells
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- Protease research in the era of systems biology
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- Association of cathepsin E with tumor growth arrest through angiogenesis inhibition and enhanced immune responses
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- Differential methylation kinetics of individual target site strands by T4Dam DNA methyltransferase
- Characterisation of zinc-binding domains of peroxisomal RING finger proteins using size exclusion chromatography/inductively coupled plasma-mass spectrometry
- Defining the extended substrate specificity of kallikrein 1-related peptidases
- Latent MMP-9 is bound to TIMP-1 before secretion
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