Scott C. Peck
Department of Biochemistry
271H Bond Life Sciences Center, University of Missouri Office phone:
(573) 882-8102 Fax:
Proteomics of protein phosphorylation and protein kinases; signaling and secretion during host-pathogen interactions.
The perception of and response to microbial signal molecules is a vital strategy evolved by plants to survive attacks by potential pathogens. Substantial evidence exists for the requirement of phosphorylation to initiate a range of defense-related responses. The identity of the phosphorylated proteins and their role in defense, however, remains largely unknown. To uncover new subsets of signaling candidates, my laboratory has developed complementary proteomic approaches to identify proteins undergoing phosphorylation in Arabidopsis cells within minutes after the application of microbial elicitors. This program has revealed more than 40 novel components associated with defense responses. We have also used reverse genetics to demonstrate that at least some of these phosphoproteins play important roles in resistance to microbes. Our next goal is to complete the pathways linking elicitor perception to the phosphorylation of these signaling components.
These initial studies on protein phosphorylation lead us to investigate the role of protein secretion in defense. We discovered a syntaxin, AtSYP132, that is essential for multiple forms of resistance to bacteria; and this syntaxin appears to be required for the secretion of antimicrobial proteins and/or compounds. A more in-depth proteomic analysis of proteins secreted during interactions between Arabidopsis and different genotypes of bacterial pathogens has revealed a complex, extracellular interaction. We are now investigating the molecular basis of these changes in protein secretion.
- Anderson JC, Bartels S, González Besteiro MA, Shahollari B, Ulm R, Peck SC. Arabidopsis MAPK Phosphatase 1 negatively regulates PAMP responses and basal resistance to Pseudomonas syringae (submitted)
- 34. Bartels S, Anderson JC, González Besteiro MA, Carreri A, Hirt H, Buchala A, Métraux J-P, Peck SC, Ulm R (2009) MAP KINASE PHOSPHATASE1 and PROTEIN TYROSINE PHOSPHATASE1 are repressors of salicylic acid and SNC1-mediated responses in Arabidopsis. Plant Cell 21:2884-2987
- Jones AME, McLean D, Studholme DJ, Serna-Sanz A, Andreasson E, Rathjen J, Peck SC (2009) Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana. J Proteomics 72: 439-451 [ScienceDirect]
- Kaffarnik FAR, Jones AME, Rathjen JP, Peck SC (2009) Effector proteins of the bacterial pathogen Pseudomonas syringae alter the extracellular proteome of the host plant, Arabidopsis thaliana.Mol Cell Proteomics 8: 145-156 [Free Access]
- Anderson JC, Peck SC (2008) A simple and rapid technique for detecting protein phosphorylation using one-dimensional isoelectric focusing gels and immunoblot analysis. Plant J 55: 881-885 [Free Access]
- Merkouropoulos G, Erik Andreasson E, Hess D, Boller T, Peck SC (2008) An Arabidopsis protein phosphorylated in response to microbial elicitation, AtPHOS32, is a Substrate of MAP Kinases 3 and 6. J Biol Chem 283: 10493-10499 [Free Access]
- Thelen J, Peck SC (2007) Quantitative Proteomics in Plants: Choices in Abundance. Plant Cell 19: 3339-3346 [Free Access]
- Nühse TS, Bottrill AR, Jones AME, Peck SC (2007) Quantitative phosphoproteomic analysis of plasma membrane proteins reveals regulatory mechanisms of plant innate immune responses. Plant J 51: 931-940 [Free Access]
- Kalde M, Nühse TS, Findley K, Peck SC (2007) The syntaxin SYP132 contributes to plant resistance against bacteria and secretion of pathogenesis-related protein 1 (PR1) Proc Natl Acad Sci USA 104: 11850-11855 [MEDLINE]