Weak oligomerization of low-molecular-weight protein tyrosine phosphatase is conserved from mammals to bacteria
| Autor: | Huimin Xu, Miquel Pons, Jascha Blobel, Pau Bernadó, Changwen Jin |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Bacteria
biology Dimer Phosphatase Active site Tyrosine phosphorylation Cell Biology Protein tyrosine phosphatase Biochemistry Evolution Molecular Molecular Weight chemistry.chemical_compound chemistry biology.protein Animals Humans Protein oligomerization Protein Multimerization Protein Tyrosine Phosphatases Tyrosine Signal transduction Molecular Biology Bacillus subtilis |
| Zdroj: | FEBS Journal. 276:4346-4357 |
| ISSN: | 1742-4658 1742-464X |
| DOI: | 10.1111/j.1742-4658.2009.07139.x |
| Popis: | 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 Bacillus subtilis, 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 association observed in vitro. Structural data suggest that substrate modulation of the oligomerization equilibrium could be a regulatory mechanism leading to the generation of signaling pulses. The presence of a phenylalanine residue in the dimerization site of YwlE, replacing a tyrosine residue conserved in all eukaryotic lmwPTPs, demonstrates that lmwPTP regulation by oligomerization can be independent from tyrosine phosphorylation. Structured digital abstract • MINT-7148507: ywle (uniprotkb:P39155) and YwlE (uniprotkb:P39155) bind (MI:0407) by nuclear magnetic resonance (MI:0077) |
| Databáze: | OpenAIRE |
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