Peter J. Kennelly
Ph.D., Biochemistry, Purdue University, 1985
B.S., Chemistry, Illinois Institute of Technology, 1978
- January 2005 – present: Head, Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg
- July 1998 – present: Professor, Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg
- July 1994 – June 1998: Associate Professor, Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg
- October 1989 – June 1994: Assistant Professor, Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg
- Mat 1985 – September 1989: Postdoctoral Research Associate, Howard Hughes Medical Institute, University of Washington School of Medicine, Seattle
Selected Major Awards
- 2010 – present: Editorial Board, Journal of Biological Chemistry
- 2010 – present: Editorial Board. Archives of Biochemistry and Biophysics
- 2010 – present: Chair, Education and Professional Development Committee, American Society for Biochemistry and Molecular Biology
- 2009 – 2013: Theme Organizer for Education and Professional Development, Annual Meeting of the American Society for Biochemistry and Molecular Biology
- 2009: Distinguished Agricultural Alumni Award, Purdue University
- 2009: Chair, Shared Instrumentation Study Section, NIH
- 1998 – 2011: Member, Fellowship Review Panel, Biochemistry, NIH (Chair 2003-05, 2007, 2008-09)
- 2009: Marquis’ Who’s Who in America
- 1997 – 2000: Department of Veteran’s Affairs Merit Review Subcommittee for General Medical Sciences
- 1996 - 2006, 2009: Awards Committee, Commonwelath of Virginia’s Alzheimer’s and Related Diseases Awards Fund
- 1996: present. Editorial Board, Analytical Biochemistry
- BCHM 4074 – Career Orientation in Biochemistry
- BCHM 2024 – Concepts of Biochemistry
Other Teaching and Advising
- Departmental Career Advisor
- Instructor in Laboratory & Radiation Safety for Incoming Graduate Students
A key event in the development of living organisms was the development of mechanisms for sensing and responding to external signals. The ability to detect nutrients and evade toxins conferred on simple unicellular organisms a massive advantage over their deaf and blind peers. The ability of cells to communicate with one another and coordinate their activities was a necessary prerequisite to the emergence of more complex organisms made up of multiple, functionally specialized cells – such as Homo sapiens. Our laboratory is using the members of the third domain of life, the Archaea, as “living fossils” for the dissecting the development of protein phosphorylation-dephosphorylation, a versatile molecular regulatory mechanism that represents one of the cornerstone building blocks for the prolific signal transduction networks in higher animals. By using phylogenetic diversity to look back over evolutionary time, we hope to map out the core of our own highly sophisticated sensor response networks. Reconstructing the development of these networks will provide useful insights into the principlaes upon which they function.
Currently, we are in the midst of identifying the protein kinases and protein phosphatases responsible for the control of protein function by phosphorylation and dephosphorylation in Sulfolobus solfataricus, an extreme acidothermophile that grows in volcanic hot springs such as those found in Yellowstone National Park. Examination of the organisms genome sequence revealed ten open reading frames encoding for plausible eukaryote-like protein kinases and two for protein phosphatases. We have expressed and characterized several of these.
Currently, we are concentrating on a set of three protein kinases that resemble the family of protein kinases in eukaryotes that shut down protein synthesis in response to nutrient deficiency, viral infection, and other stresses. The first of these, dubbed SsoPK4, phosphorylates translational initiation factor 1A, a key component in the formation of the translational initiation complex that forms as the first step in synthesizing a polypeptide from its mRNA. Interestingly, SsoPK4 is activated by oxidized Coenzyme A, a compound that accumulates in S. solfataricus when it is subject to oxidative stresses. The oxidized form of Coenzyme A is a dimer linked by an S-S bond. Analyses to date indicate that the dimeric nature of the compound is key to activation, as it serves as a bridge between two molecules of SsoPK4. When brought into close proximity to one another, each unit phosphorylates and activates the other. Current work aims to determine what signals control the other two homologues of SsoPK4 in S. solfataricus.
As chair of the education and professional development committee of the American Society for Biochemistry and Molecular Biology [ASBMB], I am a participant in national efforts by the ASBMB to improve instruction in Biochemistry, Molecular Biology and other scientific disciplines in our colleges and universities as well as in K-12 schools; and in disseminating information about career options available to students interested in Biochemistry as a profession.
- I am a member of an ASBMB team working to develop a national, outcome-based accreditation program for bachelor’s degrees in Biochemistry, Molecular Biology, and related fields.
- HOPES outreach program. The HOPES program is an ASBMB-sponsored, NSF-funded project designed to help foster the development of outreach partnerships between the members of the higher education community and K-12 teachers and their students. Each year, HOPES sponsors a workshop on the benefits and practice of K-12 outreach as part of the ASBMB’s annual meeting. The program also provides seed grants to support the efforts of higher outreach partnerships between college / university and K-12 institutions.
- In partnership with the Department of Agriculture and Extension Education and Carroll County High School, I am involved in helping develop new facilities and curriculum that will incorporate new content on the practice and application of biotechnology into the high school’s agricultural science curriculum.
- Murray, R. K., D. A. Bender, K. M. Botham, P. J. Kennelly, V. W. Rodwell, and P. A. Weil (2012) Harper’s Illustrated Biochemistry, 29th edition, McGraw-Hill Publishers, New York.
- Haile, J. D., and P. J. Kennelly (2011) “The Activity of an Ancient Atypical ProteinKinase Is Stimulated by ADP-Ribose in Vitro”, Arch. Biochem. Biophys. 511: 56-63.
- Mukhopadhyay, A., and P. J. Kennelly (2011) “A low-molecular weight proteintyrosine phosphatase from Synechocystis sp. Strain PCC 6803: Enzymaticcharacterization and identification of its potential substrates”, J. Biochem. (Tokyo),149: 551-562.
- Dahche, H., A. Abdullah, M. B. Potters, and P. J. Kennelly (2009) “A PPM-familyProtein Phosphatase from Thermoplasma volcanium Hydrolyzes Protein-boundPhosphotyrosine”, Extremophiles 13, 371-377.
- P. J. Kennelly (2008) Chapter 19, “Protein Phosphorylation at 80°C and Beyond”, Thermophiles: Biology and Technology at High Temperatures (Robb, F., Antranikian, G., Grogan, D., and Driessen, A., eds.), pp. 309-332, CRC Press, Cleveland, OH.
- (540) 231-4317