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Eliminylation: a post-translational modification catalyzed by phosphothreonine lyases
Damian F Brennan1, David Barford
1Section of Structural Biology, The Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, London, SW3 6JB, UK. damian.brennan@icr.ac.uk
Trends in Biochemical Sciences
|February 24, 2009
Summary
We introduce eliminylation, a protein modification identified in bacterial virulence factors. This process inactivates mitogen-activated protein kinases (MAPKs) and could be a widespread regulatory mechanism.
Area of Science:
- Biochemistry
- Molecular Biology
- Microbiology
Background:
- Bacterial type-III secretion systems deliver virulence factors into host cells.
- Mitogen-activated protein kinases (MAPKs) are crucial signaling proteins in eukaryotes.
- Shigella OspF and Salmonella SpvC are bacterial phosphothreonine lyases.
Purpose of the Study:
- To propose a classification for the protein post-translational modification termed eliminylation.
- To elucidate the mechanism of phosphothreonine lyases from bacterial pathogens.
- To explore the potential of phosphothreonine lyases as therapeutic agents and research tools.
Main Methods:
- Analysis of the beta-elimination reaction mechanism employed by bacterial phosphothreonine lyases.
- Investigation of the inactivation of mitogen-activated protein kinases (MAPKs).
- Identification of eliminylated residues in biological contexts like the eye lens and lantibiotics.
Main Results:
- Phosphothreonine lyases catalyze a beta-elimination reaction, removing phosphate and forming dehydrobutyrine.
- Eliminylation can also occur via decarboxylation (cysteine) or dehydration (serine, threonine).
- These modified residues are found in eukaryotic and prokaryotic systems.
Conclusions:
- Eliminylation is proposed as a novel and potentially widespread protein regulatory modification.
- Phosphothreonine lyases represent a new class of bacterial virulence factors.
- Targeting MAPKs with phosphothreonine lyases offers therapeutic potential and research applications.
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