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Faculty

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Anna C. Glasgow Karls, Ph.D.
Associate Professor and Graduate Coordinator of Microbiology
Ph.D. (1986) University of Wisconsin-Madison

Address: Department of Microbiology
255 Biological Sciences Building
Athens, GA 30602-2605
Phone: (706) 583-0822
E-mail: akarls@uga.edu
COS CV: http://myprofile.cos.com/akarls
PubMed: karls ac AND glasgow ac

Research Interests:
The research in my laboratory is on DNA rearrangements that regulate gene expression. We have identified a unique family of DNA recombinases, the Piv/MooV family that includes site-specific recombinases and transposases. We utilize genetic and biochemical approaches to determine recombination mechanisms for the Piv/MooV DNA recombinases. Our current work focuses on three members of the Piv/MooV family. Piv, a site-specific recombinase, mediates inversion of a chromosomal segment that controls expression of virulence factors in the human eye pathogen, Moraxella lacunata. MooV, a DNA transposase, catalyzes reversible excision of the transposable element IS492, which regulates extracellular polysaccharide expression in the marine biofilm-forming bacterium, Pseudoalteromonas atlantica. Irg is the transposase for ISNgo2 and ISNgo3, which are found in the pathogenic Neisseria, and may act as the integrase for the filamentous phage MDA. Definition of the molecular mechanisms for DNA recombination mediated by the recombinases of the Piv/MooV family will significantly contribute to understanding the numerous uncharacterized DNA rearrangements that are involved in medically important processes, ranging from microbial pathogenesis to oncogenesis, and may provide new targets for development of therapeutics.

Publications:
B.P. Higgins, C.D. Carpenter, and A.C. Karls. 2007. Chromosomal context directs high-frequency precise excision of IS492 in Pseudoalteromonas atlantica. PNAS 104:1901-1906.

J.M. Buchner, A.E. Robertson, D.J. Poynter, S.S. Denniston, and A.C. Karls. 2005. Piv site-specific invertase requires a DEDD motif analogous to the catalytic center of the RuvC holliday junction resolvases. J. Bacteriol. 187:3431-3437.