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Indiana University Bloomington

Department of Biology

Faculty & Research

Faculty Profile

Roger Innes

Photo of Roger Innes
Research Images
Research photo by Roger Innes

Professor of Biology
Contact Information
By telephone: 812-855-2219/5-2852(lab)
MY 316B / MY 302 (lab)

Innes Lab website

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

Research Description

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. Our research is funded by two grants from the NIH and has recently been featured in the European journal International Innovation. 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 two R genes ( RPM1 and RPS5 ) and have identified six additional genes ( PBS1 , PBS2 , PBS3 , EDR1 , EDR2 , and EDR3 ) 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 somehow activates the RPS5 protein. We are now using a combination of biochemical and genetic approaches to determine how this activation occurs. In addition, we have recently isolated a disease resistance gene from soybean, Rpg1 , that has the same specificity as RPM1 . We have shown that Rpg1 and RPM1 evolved independently in soybean and Arabidopsis, but recent data suggest that the recognition mechanism may be the same in soybean and Arabidopsis.   These analyses may allow us to develop "designer R genes" that have novel specificities for use in real world agriculture.

Select Publications
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  

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]

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]
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.
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]
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.
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.
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. 2005. Regulation of plant defense responses in Arabidopsis by EDR2, a PH and START domain-containing protein. Plant J. 44:245-257.
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.
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.

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