Weak oligomerization of low-molecular-weight protein tyrosine phosphatase is conserved from mammals to bacteria

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摘要：

The well-characterized self-association of a mammalian low-molecular-weight protein tyrosine phosphatase (lmwPTP) produces inactive oligomers that are in equilibrium with active monomers. A role of the inactive oligomers as supramolecular proenzymes has been suggested. The oligomerization equilibrium of YwlE, a lmwPTP from Bacillussubtilis, was studied by NMR. Chemical shift data and NMR relaxation confirm that dimerization takes place through the enzyme's active site, and is fully equivalent to the dimerization previously characterized in a eukaryotic low-molecular-weight phosphatase, with similarly large dissociation constants. The similarity between the oligomerization of prokaryotic and eukaryotic phosphatases extends beyond the dimer and involves higher order oligomers detected by NMR relaxation analysis at high protein concentrations. The conservation across different kingdoms of life suggests a physiological role for lmwPTP oligomerization in spite of the weak associ

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关键词：

low-molecular-weight protein tyrosine phosphatase (lmwPTP) phosphatase regulation protein oligomerization signaling pathways supramolecular proenzyme

DOI：

10.1111/j.1742-4658.2009.07139.x

年份：

2009