Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 34, Issue 3, Pages 108-114Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2008.11.005
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We propose the classification of a protein post-translational modification, eliminylation, based on the recently delineated mechanism of the Shigella OspF and Salmonella SpvC phosphothreonine Lyases. These bacterial type-III secretion-system virulence factors are injected into eukaryotic cells and inhibit signalling by irreversibly inactivating mitogen-activated protein kinases (MAPKs). Remarkably, they employ an unusual P-elimination reaction, removing the phosphate from phosphothreonine and converting it into dehydrobutyrine (an alkene). Eliminylated cysteine can also be produced by decarboxylation and eliminylated serine and threonine by dehydration; these residues are found in the eye lens and in bacterial lantibiotics. We postulate that eliminylation might be a widespread regulatory modification, and we propose the use of phosphothreonine lyases as in vivo MAPK inhibitors both therapeutically and to investigate MAPK signalling regulation.
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