Karsten W. Theis

Assistant Professor of Biochemistry and Molecular Biology, University of Massachusetts

Email: ktheis@biochem.umass.edu
K. Theis's Biochemistry and Molecular Biology Department Web Site

Ph.D.: Free University Berlin, Germany
Postdoctoral training: State University of New York at Stony Brook

DNA Repair and Molecular Motors

The focus of my laboratory is the structure of DNA motor proteins. Traveling along DNA in a unidirectional and energy-consuming manner, these molecular motors play a role in replication, transcription, recombination and repair of DNA. Failure of any one of these processes may result in cell death or uncontrolled cell growth leading to cancer. The goal of my laboratory is to obtain high resolution X-ray structures of DNA motor proteins in order to understand the common mechanism of this class of proteins (i.e. coupling of ATP hydrolysis via domain motions to DNA translocation) and how this mechanism has been adapted (e.g. in terms of DNA substrate specificity or protein-protein interactions) to give rise to distinct functions of different members of the DNA motor protein family. While the main technique of the laboratory is X-ray crystallography, techniques ranging from site-directed mutagenesis to NMR-spectroscopy will be used to complement the crystallographic data and gain a more complete understanding of the proteins and protein assemblies studied.

Representative publications:

Martin CT, Esposito EA, Theis K, Gong P. (2005) Structure and function in promoter escape by T7 RNA polymerase. Prog Nucleic Acid Res Mol Biol. 80:323-47. Review. [PubMed]

Karsten Theis, Peng Gong, and Craig T. Martin (2004) Topological and Conformational Analysis of the Initiation and Elongation Complex of T7 RNA Polymerase Suggests a New Twist
Biochemistry 43(40):12709 - 12715 [Pubmed]

James J Truglio, Deborah L Croteau, Milan Skorvaga, Matthew J DellaVecchia, Karsten Theis, Bhaskar S Mandavilli, Bennett Van Houten and Caroline Kisker (2004) Interactions between UvrA and UvrB: the role of UvrB's domain 2 in nucleotide excision repair. EMBO J. 23, 2498­2509. [Pubmed]

James J. Truglio, Karsten Theis, Yuguo Feng, Ramona Gajda, Carl Machutta, Peter J Tonge and Caroline Kisker (2003). Crystal structure of mycobacterium tuberculosis MenB, a key enzyme in vitamin K2 biosynthesis. J Biol Chem. 278:42352-42360

Milan Skorvaga, Karsten Theis, Baskhar S Mandavilli, Caroline Kisker, Bennet Van Houten. (2002) The beta -hairpin motif of UvrB is essential for DNA binding, damage processing, and UvrC-mediated incisions. J Biol Chem. 11:1553-1559

James J. Truglio, Karsten Theis, Silke Leimkuehler, Roberto Rappa, KV Rajagopalan and Caroline Kisker. (2002) Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus. Structure 10:115-125.

José A. Carrodeguas, Karsten Theis, Daniel F. Bogenhagen, and Caroline Kisker. (2001) Crystal Structure and Deletion Analysis Show that the Accessory Subunit of Mammalian DNA Polymerase, PolgB, Functions as a Homodimer. Molecular Cell 7: 43-54.

Karsten Theis, Milan Skorvaga, Mischa Machius, Noriko Nakagawa, Bennet Van Houten, Caroline Kisker. (2000) The nucleotide excision repair protein UvrB, a helicase-like enzyme with a catch. Mutat Res. 460(3-4):277-300.

Karsten Theis, Paul J. Chen, Milan Skorvaga, Bennet Van Houten and Caroline Kisker(1999) Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair. EMBO J. 18(24):6899-907.