Einstein Professor of Chemistry
Director of the Structural Biology Initiative of the CUNY Advanced Science Research Center (ASRC)
Division of ScienceDepartment
Kevin H. Gardner received his B.S. in Biochemistry from UC Davis before obtaining his Ph.D. degree in Molecular Biophysics & Biochemistry from Yale University for his research with Dr. Joseph Coleman on the development of new NMR methods to study metalloprotein structure and dynamics. Continuing his training in structural biology, he did a postdoctoral fellowship with Dr. Lewis Kay at the University of Toronto, developing novel isotopic labeling and other methods for the study of large proteins and their complexes with solution NMR. Dr. Gardner began his independent academic career at the UT Southwestern Medical Center in Dallas, where he established a structural biology research group within the Departments of Biophysics and Biochemistry, exploring regulatory mechanisms of several classes of sensory proteins and discovering ways which these may be controlled by natural or artificial stimuli in the process.
Dr. Gardner now serves as the inaugural director of the Structural Biology Initiative of the CUNY Advanced Science Research Center (ASRC) and as the Albert Einstein Professor of Chemistry at City College. The ASRC, a new 200,000 ft2 interdisciplinary research enterprise built by CUNY, assembles teams of scientists in fields that are often separated within most academic centers – structural biology, photonics, nanotechnology, neuroscience and environmental sciences – to catalyze novel collaborative interactions among experts in these fields.
postdoctoral research, University of Toronto; advisor: Lewis E. Kay, Ph.D. (1995-1998)
Ph.D., Molecular Biophysics & Biochemistry, Yale University; advisor: Joseph E. Coleman, M.D., Ph.D. (1989-1995)
B.S., Biochemistry, University of California, Davis (1985-1989)
Environmentally-regulated protein/protein interactions
Environmental cues regulate many biological processes, controlling pathways used by cells to respond to changing conditions. Such regulation is often initiated by sensory protein domains that use internally-bound ligands to convert environmentally-triggered changes into altered protein/protein interactions. Several families of these domains have evolved with remarkable diversity in the stimuli they sense and outputs that they control. Combining biophysics, biochemistry and cell biology in our group – and critically collaborating with labs in related areas – we seek insights into the signaling mechanisms of proteins used by cells to sense and respond to the environment around them. In doing so, we aim to decipher how proteins use common sensory mechanisms despite tremendous diversity in their functions and biological settings – for example, revealing how a cancer-related transcription factor in human cells senses natural metabolites similarly to a photosensory protein looking for blue light within marine bacteria. Such studies lay the foundation for both understanding the natural regulation of these systems and artificially controlling them.
Motta-Mena, L.B., Reade, A., Mallory, M.J., Glantz, S., Weiner, O.D., Lynch, K.W. and Gardner, K.H. (2014) An optogenetic gene expression system with rapid activation and deactivation kinetics. Nature Chem. Biol., 10: 196-202.
Correa, F., Ko, W.-H., Ocasio, V., Bogomolni, R.A. and Gardner, K.H. (2013) Blue light regulated two-component systems: Enzymatic and functional analysis of light-oxygen-voltage (LOV)-histidine kinases and downstream response regulators. Biochemistry, 52: 4656-4666.
Scheuermann, T.H., Li, Q., Ma, H.-W., Key, J., Zhang, L., Chen, R., Garcia, J.A., Naidoo, J., Longgood, J., Frantz, D.E., Tambar, U.K., Gardner, K.H.† and Bruick, R.K.† (2013) Allosteric inhibition of Hypoxia Inducible Factor 2 with small molecules. Nat. Chem. Biol., 9: 271-276. (†: corresponding authors).
Rivera-Cancel, G.*, Motta-Mena, L.B.* and Gardner, K.H. (2012) Identification of natural and artificial DNA substrates for the light-activated LOV-HTH transcription factor EL222. Biochemistry, 51: 10024-10034. (*: equal contributors)
Nash, A.I.*, McNulty, R.*, Shillito, M.E., Swartz, T.E., Bogomolni, R.A., Luecke, H.† and Gardner, K.H.† (2011) Structural basis of photosensitivity in a bacterial LOV-HTH DNA binding protein. Proc. Natl. Acad. Sci., 108: 9449-9454. (*: equal contributors, †: corresponding authors)
Partch, C.L. and Gardner, K.H. (2011) Coactivators necessary for transcriptional output of the hypoxia inducible factor, HIF, are directly recruited by ARNT PAS-B. Proc. Natl. Acad. Sci., 108, 7739-7744.
Zoltowski, B.D. and Gardner, K.H. (2011) Tripping the light fantastic: Blue light photoreceptors as examples of environmentally-modulated protein:protein interactions. Biochemistry, 50: 4-16.
Evans, M.R. and Gardner, K.H. (2009) Slow transition between -strand registers is dictated by protein unfolding. J. Am. Chem. Soc., 131: 11306-11307.
Wu, Q. and Gardner, K.H. (2009) BlrP1 BLUF domain: Structure and insight into light-induced changes. Biochemistry, 48: 2620-2629.
Evans, M.R., Card, P.B. and Gardner, K.H. (2009) ARNT PAS-B has a fragile native state structure with an alternative beta-sheet register nearby in sequence space. Proc. Natl. Acad. Sci., 106: 2617-2622.
Scheuermann, T.H., Tomchick, D.R., Machius, M., Guo, Y., Bruick, R.K. and Gardner, K.H. (2009) Artificial ligand binding within the HIF-2 PAS-B domain of the HIF2 transcription factor. Proc. Natl. Acad. Sci., 106: 450-455.
Yang, J., Zhang, L., Erbel, P.J.A., Gardner, K.H., Ding, K.M., Garcia, J.A. and Bruick, R.K. (2005) Functions of the Per/ARNT/Sim (PAS) domains of the hypoxia inducible factor (HIF). J. Biol. Chem., 280: 36047-36054.
Jung, A., Domratcheva, T., Tarutina, M., Wu, Q., Ko, W.-H., Shoeman, R.L., Gomelsky, M., Gardner, K.H. and Schlichting, I. (2005) Structure of a bacterial BLUF photoreceptor: Insights into blue light-mediated signal transduction. Proc. Natl. Acad. Sci. USA, 102: 12350-12355.
Harper, S.M., Christie, J.M. and Gardner, K.H. (2004b) Disruption of LOV/J helix interaction activates phototropin kinase activity. Biochemistry, 43: 16184-16192.
Harper, S.M., Neil, L.C., Day, I.J., Hore, P.J. and Gardner, K.H. (2004a) Conformational changes in a photosensory LOV domain monitored by time-resolved NMR spectroscopy. J. Am. Chem. Soc., 126: 3390-3391.
Erbel, P.J.A., Card, P.B., Karakuzu, O., Bruick, R.K. and Gardner, K.H. (2003) Structural basis for PAS domain heterodimerization in the bHLH-PAS transcription factor HIF. Proc. Natl. Acad. Sci., 100: 15504-15509.
Harper, S.M., Neil, L.C. and Gardner, K.H. (2003) Structural basis of a phototropin light switch. Science, 301: 1541-1544.
Amezcua, C.A., Harper, S.M., Rutter J. and Gardner, K.H. (2002) Structure and interactions of PAS kinase N-terminal PAS domain: Model for intramolecular kinase regulation. Structure, 10: 1349-1361.
Einstein Professor of Chemistry
2013-present, City College of New York
Excellence in Education Awards
2010, 2012 UT Southwestern Medical Center
GRC Chairs' Hall of Fame
2011, Gordon Research Conferences
Excellence in Postdoctoral Mentoring Award
2011, UT Southwestern Postdoctoral Association
Virginia Lazenby O'Hara Chair in Biochemistry
2006-2013, UT Southwestern Medical Center
Outstanding Teacher Award
2004-2005, Dept. of Biochemistry, UT Southwestern
2004, Dept. of Chemistry, University of Wisconsin
1999-2002, The Chicago Community Trust
W.W. Caruth, Jr. Scholar in Biomedical Research
1998-2013, UT Southwestern Medical Center
Helen Hay Whitney Postdoctoral Fellow
1996-1998, Helen Hay Whitney Foundation
NIH/NRSA Postdoctoral Fellow
1995-1996, National Institutes of Health
HHMI Predoctoral Fellow
B.S. with Highest Honors (Biochemistry)
1989, UC Davis
Departmental Citation for Excellence
1989, UC Davis, Department of Biochemistry
Phi Beta Kappa
1989, UC Davis