Weak oligomerization of low-molecular-weight protein tyrosine phosphatase is conserved from mammals to bacteria
- 影响因子：
0.0
- 发表刊物：
FEBS J
- 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 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.
- 论文类型：
期刊论文
- 论文编号：
28
- 卷号：
276
- 页面范围：
4346-4357
- ISSN号：
16
- 是否译文：
否
- 发表时间：
2009-08-01
- 收录刊物：
SCI
- 发布期刊链接：
- 第一作者：
Jascha Blobel
- 通讯作者：
Miquel Pons
- 全部作者：
Pau Bernadó,Huimin Xu,Changwen Jin
