Biochemistry

Scott C. Peck

Associate Professor of Biochemistry

E-mail:pecks@missouri.edu

Office: 271H Bond Life Sciences Center

Mail: Christopher S. Bond Life Sciences Center
271H Bond Life Sciences Center
University of Missouri
Columbia, MO 65211

Phone: 573-882-8102

Fax: 573-884-9676

Lab: 573-882-7431

Educational background

Curriculum vitae

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Notable honors and service

• BMC Plant Techniques, Co-Editor
• The Plant Cell, Co-Editor

Research summary

We study how potential hosts recognize and respond to invading microbes, particularly bacteria. Using proteomic and phosphoproteomic approaches, we have identified numerous proteins involved in cellular signaling and protein secretion. We are currently using a diverse platform of biochemical and genetic approaches to investigate the functions of these proteins.

Research description

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.

We also have collaborative projects to investigate:

• changes in protein phosphorylation that may be involved in hyphal development of Candida albicans, a fungal pathogen of humans;
• the potential role Zn2+ as a secondary messenger during inflammatory responses to bacterial lipopolysaccharides in murine macrophage cells; and
• changes in protein phosphorylation in Salmonella typherium during infection.

Selected publications

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]

Nühse TS, Stansballe A, Jensen ON, Peck SC (2004) Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database. Plant Cell 16: 2394-2405 [Free Access]

Lab members

Postdoctoral fellows:

Jeff Anderson
role of phosphatases in signaling/signaling leading to systemic recombination

Bationa Shahollari
kinase-substrate interactions during plant innate immune responses

Jenny Zhang
development of quantitative proteomics approaches to study membrane dynamics/ phosphoproteomics of systemic recombination signaling

Graduate students

Ying Wan
Zn2+ as a potential second messenger in mammalian macrophage cells

Holly Ziobro
characterization of factors from bacterial pathogens that alter protein secretion in the host

Undergraduate students

George Cyriac
analysis of SYP132-interacting proteins

Jarrod Dye
characterization of differential responses to microbial elicitors

Employment opportunities

Postdoctoral opportunities

Research areas: Proteomics of protein phosphorylation and protein kinases; signaling and secretion during host-pathogen interactions.

How to apply:

Electronic submission is encouraged, e-mail to pecks@missouri.edu

Applicants should send CV and names of two references to:
Dr. Scott C. Peck
Christopher S. Bond Life Sciences Center
271H Bond Life Sciences Center
University of Missouri
Columbia, MO 65211