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James Bowie

Website:

James Bowie's Home Page.

Work Email Address:

bowie@mbi.ucla.edu

Laboratory Address:

Paul Boyer Hall 659

Work Address:

Paul Boyer Hall 655

Work Phone Number:

1 (310) 206-4747
1 (310) 206-7481
Professor
Chemistry and Biochemistry, UCLA-DOE Institute for Genomics & Proteomics, Molecular Biology Institute
Member
Biochemistry & Molecular Biology (BMB) Graduate Program

A Short Biography:

B.A. Carleton College 1981; Ph.D. MIT 1989; Life Sciences Research Council Postdoctoral Fellow, 1989-92; American Cancer Society Postdoctoral Fellow, 1992-3; Assistant Professor, Chemistry and Biochemistry, UCLA, 1993-2000, Associate Professor, Chemistry and Biochemistry, UCLA, 2000-04, Professor, Chemistry and Biochemistry, 2004-present. Protein Society Executive Council (2006-), Editorial Board of Journal of Molecular Biology (2006-), Biochemistry (2006-), Protein Science (2000-) and Proteins (1997-2005), Advisory Board Swedish Biomembrane Center (2005-), Co-chair FASEB summer conference on Mol. Biophys. Cell. Membranes (2006&08). Co-chair Gordon Conference on Proteins (2010&12), Member NIH BBM study section (2006-) Temporary Member NIH BBCB (2001), NIH Biochemistry(2000, 2002) and NIH BBM (2005) Study Sections

Click here for information about the Biochemistry and Molecular Biology (BMB) Graduate Program.

Awards and Honors:

1994 NSF National Young Investigator ; 1994 Pew Scholar ; 1998 McCoy Award in Chemistry ; 2001 Leukemia & Lymphoma Society Scholar ; American Cancer Society Postdoctoral Fellowship ; Life Science Research Foundation Postdoctoral Fellowship

Research Interest:

Membrane Protein Structure

A third of all proteins and the vast majority of drug targets are membrane proteins. In spite of their biological and medical importance, our understanding of membrane protein structure and function is still at a rudimentary level and our tools for working with membrane proteins are primitive. The questions we are addressing in this area are:

  • Can we develop better techniques for membrane protein expression?
  • Can we develop better techniques for membrane protein crystallization?
  • How are membrane protein structures defined by their amino acid sequence?
  • Can we learn to predict membrane protein structure?

SAM Domains: A Biological Polymer

SAM domains are one of the most common protein modules found in eukaryotic cells. We discovered that many SAM domains can form polymers, establishing the existence of a new biological polymer that can be used to build complex biological structures. The questions we address in this area are:

  • What structures can SAM domain polymers form?
  • What are the biological roles of SAM polymers?
  • How can SAM polymerization be regulated?
  • How can SAM polymers be used in bio-engineering applications?

Bioenergy

Developing new sources of energy is a grand challenge for science in the coming decades. We are working to utilize micro-organisms to convert carbon dioxide and light into biodiesel.


Detailed Biography:

Bowie got hooked on proteins at an early age and never looked back. The obsession began as a high school student when he did a research project on blood clotting enzymes with Kenneth G. Mann at the Mayo Clinic in his hometown of Rochester, MN. The research project won him a trip to the International Science and Engineering fair and a Westinghouse Award, experiences that further stimulated his interest in science. He went on to Carleton College, where he got a B. A. degree in Chemistry with Distinction. He did research in carbohydrate chemistry with Gary R. Gray at the University of Minnesota before entering graduate school at M.I.T. There he returned to proteins in the laboratory of Robert T. Sauer, using experimental and computational methods to probe and predict protein structure. After completing his Ph.D. work, he did postdoctoral work with David Eisenberg at UCLA, continuing work on structure prediction and structure determination by x-ray crystallography. He joined the UCLA faculty in 1993 and is now a full professor.

Publications:

Joh Nathan Hyunjoong, Min Andrew, Faham Salem, Whitelegge Julian P, Yang Duan, Woods Virgil L, Bowie James U   Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins. Nature, 2008; 453(7199): 1266-70.
Harada Bryan T, Knight Mary Jane, Imai Shin-Ichi, Qiao Feng, Ramachander Ranjini, Sawaya Michael R, Gingery Mari, Sakane Fumio, Bowie James U   Regulation of enzyme localization by polymerization: polymer formation by the SAM domain of diacylglycerol kinase delta1. Structure, 2008; 16(3): 380-7.
Gorman Paul M, Kim Sanguk, Guo Meng, Melnyk Roman A, McLaurin Joanne, Fraser Paul E, Bowie James U, Chakrabartty Avijit   Dimerization of the transmembrane domain of amyloid precursor proteins and familial Alzheimer's disease mutants. J. Mol. Biol., 2008; 9(4): 17.
Sapra K Tanuj, Balasubramanian G Prakash, Labudde Dirk, Bowie James U, Muller Daniel J   Point mutations in membrane proteins reshape energy landscape and populate different unfolding pathways. J. Mol. Biol., 2008; 376(4): 1076-90.
Nauli Sehat, Farr Saman, Lee Yueh-Jung, Kim Hye-Yeon, Faham Salem, Bowie James U   Polymer-driven crystallization. Protein Sci., 2007; 16(11): 2542-51.
Plotkowski Megan L, Kim Sanguk, Phillips Martin L, Partridge Anthony W, Deber Charles M, Bowie James U   Transmembrane domain of myelin protein zero can form dimers: possible implications for myelin construction. Biochemistry, 2007; 46(43): 12164-73.
Pettit Frank K, Bare Emiko, Tsai Albert, Bowie James U   HotPatch: a statistical approach to finding biologically relevant features on protein surfaces. J. Mol. Biol., 2007; 369(3): 863-79.
Barwe Sonali P, Kim Sanguk, Rajasekaran Sigrid A, Bowie James U, Rajasekaran Ayyappan K   Janus model of the Na,K-ATPase beta-subunit transmembrane domain: distinct faces mediate alpha/beta assembly and beta-beta homo-oligomerization. J. Mol. Biol., 2007; 365(3): 706-14.
Oberai Amit, Ihm Yungok, Kim Sanguk, Bowie James U   A limited universe of membrane protein families and folds. Protein Sci., 2006; 15(7): 1723-34.
Gundelfinger Eckart D, Boeckers Tobias M, Baron Marisa K, Bowie James U   A role for zinc in postsynaptic density asSAMbly and plasticity? Trends Biochem. Sci., 2006; 31(7): 366-73.
Bowie James U   Flip-flopping membrane proteins. Nat. Struct. Mol. Biol., 2006; 13(2): 94-6.
Baron Marisa K, Boeckers Tobias M, Vaida Bianca, Faham Salem, Gingery Mari, Sawaya Michael R, Salyer Danielle, Gundelfinger Eckart D, Bowie James U   An architectural framework that may lie at the core of the postsynaptic density. Science, 2006; 311(5760): 531-5.
Qiao Feng, Harada Bryan, Song Haiyun, Whitelegge Julian, Courey Albert J, Bowie James U   Mae inhibits Pointed-P2 transcriptional activity by blocking its MAPK docking site. EMBO J., 2006; 25(1): 70-9.
Bowie James U   Solving the membrane protein folding problem. Nature, 2005; 438(7068): 581-9.
Kim Sanguk, Jeon Tae-Joon, Oberai Amit, Yang Duan, Schmidt Jacob J, Bowie James U   Transmembrane glycine zippers: physiological and pathological roles in membrane proteins. Proc. Natl. Acad. Sci. U.S.A., 2005; 102(40): 14278-83.
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