Faculty & Research
- Contact Information
- Contact Roger Innes by rinnes [at] indiana [dot] edu
- By telephone: 812-855-2219/5-2852(lab)
- MY 316B / MY 302 (lab)
- Genome, Cell & Developmental Biology
- Research Areas
- Eukaryotic Cell Biology, Cytoskeleton and Signaling
- Microbial Interactions and Pathogenesis
- Plant Molecular Biology
Ph.D., University of Colorado, 1988 Postdoctoral Fellow, University of California, Berkeley, 1988-91
American Association for the Advancement of Science Fellow
American Academy of Microbiology Fellow
Our primary interest is in understanding the genetic and biochemical basis of disease resistance in plants. Plants are able to specifically recognize pathogens and actively respond. We are investigating how this specific recognition is accomplished and how recognition is translated into a resistant response. To address these questions we take a molecular genetic approach. We use the small mustard Arabidopsis thaliana as our standard host plant, and the bacterial pathogen Pseudomonas syringae as our standard pathogen. Recognition of specific P. syringae strains by Arabidopsis is mediated by specific disease resistance (R) genes of Arabidopsis. These R genes are thought to encode receptors that detect a signal produced directly or indirectly by bacterial proteins that are injected into the plant cell. The molecular mechanism of this detection step is poorly understood, however. Understanding this mechanism is a major goal in plant biology as it will likely lead to new approaches for engineering disease resistance in plants, as well as provide critical insights into how pathogens evolve to escape recognition and cause disease. To uncover the molecular basis of pathogen recognition we have focused on identifying genes in both the plant and the pathogen that are required for the recognition event. This has been accomplished by screening for plant mutants that fail to respond to bacteria expressing specific effector proteins that are secreted into the plant cells. To date we have cloned four R genes (RPM1 and RPS5 from Arabidopsis and Rpg1b and Rpg1r from soybean) and have identified seven additional genes (PBS1 , PBS2 , PBS3 , EDR1 , EDR2 , EDR3, and KEG) believed to mediate signal transduction events. RPM1 and RPS5 belong to a very large gene family in plants. Each member of this family mediates recognition of a specific pathogen molecule. All members of this R gene family contain a nucleotide binding site (e.g. ATP) and leucine rich repeats (LRRs). The LRRs are thought to mediate protein:protein interactions, and may possibly participate in binding pathogen molecules or the targets of pathogen molecules. We have shown that the PBS1 protein is a target of the P. syringae protease AvrPphB, and that cleavage of PBS1 activates the RPS5 protein as a result of conformational changes in PBS1. Most recently, we have shown that PBS1 can be modified so that it becomes a ‘decoy’ target for other pathogen proteases, which then enables RPS5 to recognize other pathogens, including viruses. These analyses may allow us to develop "designer R genes" that have novel specificities for use in real world agriculture.
- Qi, D., U. Dubiella, S. H. Kim, D. I. Sloss, R. H. Dowen, J. E. Dixon and R. W. Innes. 2013. Recognition of the protein kinase PBS1 by the disease resistance protein RPS5 is dependent on S-acylation and an exposed loop in PBS1. Plant Physiol. PMID:24225654
- Gu, Y. and R. W. Innes. 2012. The KEEP ON GOING (KEG) protein of Arabidopsis regulates intracellular protein trafficking and is degraded during fungal infection. Plant Cell, 24: 4717-4730 [article]
Qi, D., B.J. DeYoung, and R. W. Innes. 2012. Structure-function analysis of the coiled-coil and leucine-rich repeat domains of the RPS5 disease resistance protein. Plant Physiol. 158: 1819-1832. [article]
- Wawrzynska, A., K. M. Christiansen, Y. Lan, N. L. Rodibaugh and R. W. Innes 2008. Powdery Mildew Resistance Conferred by Loss of the EDR1 Protein Kinase is Suppressed by a Missense Mutation in KEG, a Regulator of ABA Signaling. Plant Phys. 148: 1510-1522 [article]
- Innes, R. W., C. Ameline-Torregrosa, T. Ashfield, E. Cannon, S. B. Cannon, B. Chacko, N. W. G. Chen, A. Couloux, A. Dalwani, R. Denny, S. Deshpande, A. Egan, N. Glover, C. S. Hans, S. Howell, D. Ilut, S. Jackson, H. Lai, J. Mammadov, S. M. d. Campo, M. Metcalf, A. Nguyen, M. O’Bleness, B. Pfeil, R. Podicheti, M. B. Ratnaparkhe, S. Samain, I. Sanders, B. Ségurens, M. Sévignac, S. Sherman-Broyles, V. Thareau, D. M. Tucker, J. Walling, A. Wawrzynski, J. Yi, J. J. Doyle, V. Geffroy, B. A. Roe, M. A. S. Maroof and N. D. Young 2008. Differential accumulation of retroelements and diversification of NB-LRR disease resistance genes in duplicated regions following polyploidy in the ancestor of soybean. Plant Phys. 148: 1740-1759.
- Ade, J., B. J. DeYoung, C. Golstein and R. W. Innes. 2007. Indirect activation of a plant NBS-LRR protein by a bacterial protease. Proc. Natl. Acad. Sci. USA. 104: 2531-2536.
- Ong, L.E. and R. W. Innes 2006. AvrB mutants lose both virulence and avirulence activities on soybean and Arabidopsis. Mol. Micro. 60:951-962.
- Tang, D., J. Ade, C. A. Frye and R. W. Innes. 2006. A mutation in the GTP hydrolysis site of Arabidopsis Dynamin-Related Protein 1E confers enhanced cell death in response to powdery mildew infection. Plant J. 47:75-84.
- Tang, D., K. Christiansen and R. W. Innes. 2005. Regulation of plant disease resistance, stress responses, cell death and ethylene signaling in Arabidopsis by the EDR1 protein kinase. Plant Phys. 138: 1018-1026.
- Tang, D., J. Ade, C. A. Frye and R. W. Innes. 2005. Regulation of plant defense responses in Arabidopsis by EDR2, a PH and START domain-containing protein. Plant J. 44:245-257.
- Ashfield, T., L. Ong, C. M. Scheider and R. W. Innes. 2004. Convergent evolution of disease resistance gene specificity in two flowering plant families. Plant Cell, 16:309-318.
- Shao, F., C. Golstein, J. Ade, M. Stoutemyer, J. Dixon and R. Innes 2003. Cleavage of Arabidopsis PBS1 by a bacterial type III effector. Science, 301:1230-1233.
- Shao, F., P.M.Merritt, Z. Bao, R.W. Innes and J.E. Dixon. 2002. A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis. Cell, 109: 575-588.