TAILIEUCHUNG - Báo cáo khoa học: Weak oligomerization of low-molecular-weight protein tyrosine phosphatase is conserved from mammals to bacteria

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 oligo-mers as supramolecular proenzymes has been suggested. | Weak oligomerization of low-molecular-weight protein tyrosine phosphatase is conserved from mammals to bacteria Jascha Blobel1 Pau Bernado1 Huimin Xu2 Changwen Jin2 and Miquel Pons1 3 1 Laboratory of Biomolecular NMR Institute for Research in Biomedicine Barcelona Spain 2 Beijing Nuclear Magnetic Resonance Center College of Life Sciences College of Chemistry and Molecular Engineering Peking University Beijing China 3 Departament de Quimica Organica Universitat de Barcelona Spain Keywords low-molecular-weight protein tyrosine phosphatase lmwPTP phosphatase regulation protein oligomerization signaling pathways supramolecular proenzyme Correspondence M. Pons Laboratory of Biomolecular NMR Institute for Research in Biomedicine Parc Cientific de Barcelona Baldiri Reixac 10 08028 Barcelona Spain Fax 34934039976 Tel 34934034683 E-mail mpons@ Received 13 April2009 revised 5 June 2009 accepted 9 June 2009 doi 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

• Báo cáo khoa học
• medical report
• Scientific reports
• scientific research
• tumor cells
• medical knowledge
• chemical reaction
• thesis report
• medical research
• analysis of cytoplasmic
• Nobel Prizes
• health technologies
• medical ebook
• medical document
• medical specific study
• Crystal structure
• medical analysis
• biochemical studies
• intermediate cells
• cell proliferation
• cytoplasm