Dr. John L. Spudich, Professor and Robert A. Welch
Distinguished Chair in Chemistry

Director, Center for Membrane Biology
Department of Biochemistry and Molecular Biology
Program in Biochemistry and Molecular Biology

University of Texas-Houston Medical School
P.O. Box 20708 - Houston, Texas 77225
(713) 500-5473 fax:(713)500-0545
email: John.L.Spudich@uth.tmc.edu

Ph.D, University of California, Berkeley
Jane Coffin Childs Postdoctoral Fellow, Harvard Medical Schoolschl Career Scientist Award, NIH Merit Award

membrane protein structure and function

Membrane Protein Structure and FunctionThe primary interest in our laboratory is the mechanism by which photosensory receptors sense and transmit information concerning the color, intensity, and pattern of light in the environment. We study a widespread class of photoactive receptor proteins (rhodopsins) that consist of seven transmembrane helices connected by interhelical loops. The helices form a pocket for the photosensitive molecule vitamin-A aldehyde (retinal), and the receptor proteins physically couple to protein transducers that relay signals to sensory pathways in the cytoplasm. These photosensitive heptahelical proteins are used for visual processes of various degrees of sophistication, ranging from detection of light-dark boundaries, light gradients, and light direction by single-cell microorganisms to high-resolution color image detection by higher animal eyes

Sudo, Y. and Spudich, J.L. (2006) Three strategically placed hydrogen-bonding residues convert a proton pump into a sensory receptor. Proc. Natl. Acad. Sci. USA 103, 16129-16134.

Sudo, Y., Furutani, Y., Kandori, H., Spudich, J.L. (2006) Functional importance of the interhelical  hydrogen  bond  between Thr204 and Tyr174 of sensory rhodopsin II and its alteration during the signaling process. J. Biol. Chem. 281, 34239-34245.

Spudich, J.L. (2006) The multilalented microbial sensory rhodopsins. Trends Microbiol. 14, 480-487.

Bergo, V.B., Ntefidou, M. Trivedi, V.D. Amsden, J.J., Kralj, J.M., Rothschild, K.J., Spudich, J.L. (2006) Conformational changes in the photocycle of Anabaena sensory rhodopsin.  J. Biol. Chem. 281:5208-15214.

Bergo, V.B., Spudich, E.N, Rothschild, K.J., and Spudich, J.L. (2005) Photoactivation perturbs the membrane-embedded contacts between sensory rhodopsin II and its transducer. J. Biol. Chem. 280, 28365-28369.

Vogeley, L., Sineshchekov, O.A., Trivedi, V.D., Sasaki, J., Spudich, J.L. and Luecke, H. (2004) Anabaena Sensory Rhodopsin: A Photochromic Color Sensor at 2.0 Å. Science. 306, 1390-1393.

Sineshchekov, O.A., Jung, K.-H., and Spudich, J.L. (2002) Two rhodopsins mediate phototaxis to low and high intensity light in Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA 99, 8689-8694.

Luecke, H., Schobert, B., Lanyi, J.K., Spudich, E.N., and Spudich, J.L. (2001) Crystal Structure of Sensory Rhodopsin II at 2.4 Å: Insights into Color Tuning and Transducer Interaction. Science 293, 1499-1503.

Béjà*, O., Spudich*, E.N., Spudich, J.L., Leclerc, M., and DeLong, E.F. (2001) Proteorhodopsin phototrophy in the ocean.  Nature 411, 786-789 {*1st  two authors equal contributors}.

Spudich, J.L., Yang, C.-H., Jung, K.-H., and Spudich, E.N. (2000) Retinylidene Proteins: Structures and Functions from Archaea to Humans. Annual Reviews Cell & Dev. Biol. 16, 365-392.