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Pathogens use previously undescribed mechanism to sabotage host immune system
Date:12/7/2007

al flexibility for this interaction. The researchers went on to identify a previously unknown catalytic mechanism of acid-base mediated "-elimination of phosphoserine/phosphothreonine that irreversibly inactivated the kinase.

Our data provide biochemical and structural evidence for specific recognition of the dual phosphorylated MAPK substrates by the OspF family of phosphothreonine lyases and explain the enzymes differential activities towards different MAPK substrates, explains Dr. Shao. Further, as phosphorylation of serine and threonine residues is widely used as a regulatory mechanism in mammalian cells, the researchers speculated that phosphoserine or phosphothreonine lyases might exist in eukaryotes and serve as post-translational modification enzymes that irreversible dephosphorylate kinases or other phosphorylated substrates.


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Contact: Cathleen Genova
cgenova@cell.com
617-397-2802
Cell Press
Source:Eurekalert

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