- Undergraduate Education
- B.A Rice University (1989)
- Graduate Education
- Ph.D. University of California at Berkeley (1995)
- Postdoc. Yale University Medical School, New Haven, CT (1995-2000)
- Assistant Professor, Princeton Univ. 2001-2009
- Joined Texas A&M in 2009
Molecular Chaperones in protein and membrane dynamics
A fundamental principle of biology is the use of chemical energy in the form of ATP to assemble, disassemble and alter macromolecular structure. Specialized control proteins known as molecular chaperones are often responsible for this activity and have been recognized in recent years to be essential for regulating many aspects of cellular biology. Using a variety of biophysical and biochemical techniques, the Rye lab focuses on three fundamental cellular processes that require molecular chaperones: (1) protein folding (2) protein disaggregation and (3) vesicle trafficking. In each of these cases, large quantities ATP are burned, resulting in molecular organization in the case of protein folding, and molecular disassembly and remodeling in the case of protein disaggregation and vesicle trafficking. We are interested in understanding the detailed biophysical mechanisms that underpin these events. Why are these processes so energetically expensive? Are there any similarities in how the energy is used between these very different molecular processes? Are there general principles of energy transduction in biology that can be gleaned by comparing these examples with other molecular machines, such as cytoskeletal motors? Understanding how molecular chaperones control protein and membrane organization will provide key insights into not only basic cell biology, but will also illuminate aspects of many diseases that spring from aberrant protein and membrane dynamics.
Brooks, A, Shoup, D, Kustigian, L, Puchalla, J, Carr, CM, Rye, HS et al.. Single particle fluorescence burst analysis of epsin induced membrane fission. PLoS ONE. 2015;10 (3):e0119563.
Weaver, J, Watts, T, Li, P, Rye, HS. Structural basis of substrate selectivity of E. coli prolidase. PLoS ONE. 2014;9 (10):e111531.
Weaver, J, Rye, HS. The C-terminal tails of the bacterial chaperonin GroEL stimulate protein folding by directly altering the conformation of a substrate protein. J. Biol. Chem. 2014;289 (33):23219-32.
Lin, Z, Puchalla, J, Shoup, D, Rye, HS. Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding. J. Biol. Chem. 2013;288 (43):30944-55.
Krantz, KC, Puchalla, J, Thapa, R, Kobayashi, C, Bisher, M, Viehweg, J et al.. Clathrin coat disassembly by the yeast Hsc70/Ssa1p and auxilin/Swa2p proteins observed by single-particle burst analysis spectroscopy. J. Biol. Chem. 2013;288 (37):26721-30.
Chen, DH, Madan, D, Weaver, J, Lin, Z, Schröder, GF, Chiu, W et al.. Visualizing GroEL/ES in the act of encapsulating a folding protein. Cell. 2013;153 (6):1354-65.
Karuri, NW, Lin, Z, Rye, HS, Schwarzbauer, JE. Probing the conformation of the fibronectin III1-2 domain by fluorescence resonance energy transfer. J. Biol. Chem. 2009;284 (6):3445-52.
Madan, D, Lin, Z, Rye, HS. Triggering protein folding within the GroEL-GroES complex. J. Biol. Chem. 2008;283 (46):32003-13.
Lin, Z, Madan, D, Rye, HS. GroEL stimulates protein folding through forced unfolding. Nat. Struct. Mol. Biol. 2008;15 (3):303-11.
Lin, Z, Rye, HS. GroEL-mediated protein folding: making the impossible, possible. Crit. Rev. Biochem. Mol. Biol. ;41 (4):211-39.