Biotechnology Center for Agriculture and the Environment
Foran Hall, 59 Dudley Road
New Brunswick, NJ 08901-8520
(732) 932-8165 x320
Fax: (732) 932-0312
zylstra@aesop.rutgers.edu
Home Page: www.rci.rutgers.edu/~zylstraProfessor of Microbiology
Director of the Biotech Center
B.S. (Biology), Calvin College, 1981
Ph.D. (Cellular & Molecular Biology), University of Michigan, 1987
Molecular and biochemical basis for microbial aromatic hydrocarbon degradation
Research in my laboratory is directed toward understanding the mechanisms by which different bacterial strains utilize aromatic compounds as carbon and energy sources. Projects in the laboratory emphasize the use of molecular genetic tools in the analysis of gene (and protein) evolution, the regulation of gene expression, the identification of intermediate compounds in catabolic pathways, and the functional analysis of the enzymes involved. The primary theme for projects in the laboratory is the examination of microbial diversity and how this affects the degradation of aromatic compounds in the environment. For instance, different bacterial strains may utilize different biochemical pathways for the degradation of the same aromatic compound. In contrast, different bacterial strains may degrade an aromatic compound by the same catabolic pathway but possess genes that have diverged widely in their nucleotide sequence. This diversity in nucleotide sequence also plays a role in the specificity and activity of the enzymes produced. Research thus focuses on a detailed biochemical, physiological, and molecular genetic investigation and comparison of different model catabolic pathways in different bacterial genera. Specific areas of research include: (1) site-directed modification of enzymes to understand their function and to perhaps enhance their ability to transform aromatic compounds to oxygenated intermediates, (2) analysis of gene regulation and how this can be used to enhance microbial biodegradation of xenobiotic compounds in the environment, (3) design and use of molecular probes to track genes and their expression in the environment, and (4) construction of hybrid catabolic pathways for the degradation of recalcitrant compounds. The laboratory is currently focusing on the degradation of polycyclic aromatic hydrocarbons by Sphingomonas, Comamonas, and Mycobacterium strains, the degradation of nitrophenols and nitrobenzoates by several different Pseudomonas species, and the degradation of phthalates by P. cepacia, C. testosteroni, and Acinetobacter.
RECENT PUBLICATIONS
Chae, J.-C., E. Kim, E. Bini, and G. J. Zylstra. 2007. Comparative analysis of the catechol 2,3-dioxygenase gene locus in thermoacidophilic archaeon Sulfolobus solfataricus strain 98/2. Biochem. Biophys. Res. Commun. 357:815-819.
Yano, H., C. E. Garruto, M. Sota, Y. Ohtsubo, Y. Nagata, G. J. Zylstra, P. A. Williams, and M. Tsuda. 2007. Complete sequence determination combined with analysis of transposition/site-specific recombination events to explain genetic organization of the IncP-7 TOL plasmid pWW53 and related mobile genetic elements. J. Mol. Biol. 25:11-26.
Wawrik, B., D. Kutliev, U. A. Abdivasievna, J. J. Kukor, G. J. Zylstra, and L. J. Kerkhof. 2007. Biogeography of Actinomycete communities and Type II polyketide synthase genes in soils collected in New Jersey and Central Asia. Appl. Environ. Microbiol. 73:2982-2989.
Poulain, A. J., S. M. Ní Chadhain, P. A. Ariya, M. Amyot, E. Garcia, P. G. Campbell, G. J. Zylstra, and T. Barkay. 2007. Potential for mercury reduction by microbes in the high arctic. Appl. Environ. Microbiol. 73:2230-2238.
Rhine, E. D., S. M. Ní Chadhain, G. J. Zylstra, and L. Y. Young. 2007. The arsenite oxidase genes (aroAB) in novel chemoautotrophic arsenite oxidizers. Biochem. Biophys. Res. Commun. 354:662-667.
Rozhkova-Novosad, E. A., J.-C. Chae, G. J. Zylstra, E. M. Bertrand, M. Alexander-Ozinskas, D. Deng, L. A. Moe, J. B. van Beilen, M. Danahy, J. T. Groves, and R. N. Austin. 2007. Profiling mechanisms of alkane hydroxylase activity in vivo using the diagnostic substrate norcarane. Chemical Biology 14:165-172.
Yu, C. L., W. Liu, D. J. Ferraro, E. N. Brown, J. V. Parales, S. Ramaswamy, G. J. Zylstra, D.T. Gibson and R.E. Parales. 2007. Purification, characterization, and crystallization of the components of a biphenyl dioxygenase system from Sphingobium yanoikuyae B1. J. Ind. Microbiol. Biotechnol. 34:311-324.
Choi, K. Y., D. Kim, J.-C. Chae, G. J. Zylstra, E. Kim. 2007. Requirement of duplicated operons for maximal metabolism of phthalate by Rhodococcus sp. strain DK17. Biochem. Biophys. Res. Commun. 357:766-771.
Kim, D., J. S. Lee, K. Y. Choi, Y.-S. Kim, J. N. Choi, S.-K. Kim, J.-C. Chae, G. J. Zylstra, C. H. Lee, and E. Kim. 2007. Effect of substituent size on the regioselectivity of a novel o-xylene dioxygenase from Rhodococcus sp. strain DK17. Enz. Microb. Tech. 41:221-225.
Choi, K. Y., G. J. Zylstra, and E. Kim. 2007. Benzoate catabolite repression of the phthalate degradation pathway in Rhodococcus sp. strain DK17. J. Bact. 73:1370-1374.
Bae, H. W., D. Kim, K. Y. Choi, N. R. Kwon, J.-C. Chae, G. J. Zylstra, S.-C. Koh, C.-H. Lee, and E. Kim. 2007. Functional identification of p-cumate operons in the terpene-degrading Rhodococcus sp. strain T104. FEMS Microbiol. Lett. 266:55-59.
