Willem F. J. Vermaas
Wim Vermaas came to Arizona State University in 1986 after having worked on various aspects of plant cell and molecular biology at the University of Illinois, Michigan State University, the Technical University in Berlin (Germany), the Agricultural University in Wageningen (The Netherlands), and the Du Pont Experimental Station (Wilmington, Delaware). Since coming to ASU, research in his group has focused on the molecular biology and cell physiology of prokaryotic photosynthetic systems, increasingly making use of functional genomics. Dr. Vermaas is involved with the National Science Foundation (NSF) supported Integrative Graduate Education and Research Training (IGERT) program in Biomolecular Nanotechnology, and was Director of the related NSF-supported Graduate Research Training Program in the molecular plant sciences. Moreover, Dr. Vermaas has coordinated of the US Department of Energy supported Genomes-to-Life Project on the cyanobacterium Synechocystis sp. PCC 6803.
The central, broad research focus in our group is to try to understand the physiology of a bacterium based on genomic and other information. This broad field, often referred to as functional genomics, uses complete genome sequences and integrates this with information from the protein composition of the organism (proteome) and the organic compounds in the cell (metabolome). Based on the genome sequence, a network of pathways and regulation in the organism can be deduced, which can then be tested and refined experimentally. This interdisciplinary research field thus integrates molecular biology with chemistry and biochemistry to provide answers that are relevant at the cell-physiological level.
Our group, consisting of a balanced mix of graduate students, postdoctoral associates, staff, and undergraduate students, utilizes a cyanobacterium by the name of Synechocystis sp. PCC 6803 ( Synechocystis for short). Cyanobacteria are a group of very versatile and ancient organisms that can grow under a large range of conditions and that have many ways to make a living. The reason for using Synechocystis is that its photosynthetic system is essentially identical to that of plants; moreover -- in contrast to most "real" plants -- it is a molecular biologist's dream: its genome (some 3.6 million base pairs) has been sequenced in its entirety, it is spontaneously transformable (i.e., it takes up DNA by itself), it can integrate DNA into its genome by homologous recombination, and it can grow in the absence of photosynthesis if it needs to.
Using this system, we can take out specific genes or put back in genes with particular modifications or novel genes from other organisms. We then can study the in vivo effects of the lack modification, or introduction of the corresponding protein on the physiology of the organism. This research helps to build a fundamental understanding regarding how changes in levels or activities of particular proteins translate to alterations in the physiology of the organism. Possibilities for research projects with the Synechocystis 6803 system are almost unlimited. Just a few examples: we are using this system to study the interaction between chlorophyll synthesis and assembly of chlorophyll-binding complexes, to identify protein residues in specific polypeptides that are of functional importance, to find "new" genes that affect and regulate photosynthesis and respiration or that are involved in biosynthesis of unique carotenoids, to elucidate unusual aspects of the "metabolome" of this cyanobacterium, to determine how thylakoid membranes are synthesized, and to develop new molecular-biological tools to study protein structure and function. Moreover, we put together this information to develop an understanding of the molecular physiology of the cyanobacterial cell. This research has many potential implications, ranging from metabolic engineering opportunities (solar energy conversion into hydrogen or other fuels, or production of bioplastics) to new evolutionary insights. It is an exciting field of research, providing students with excellent interdisciplinary research training opportunities in the molecular life sciences.
Selected Publications
Kufryk, G.I., and Vermaas, W.F.J. (2006) Sll1717 in Synechocystis sp. PCC 6803 affects the redox state of the plastoquinone pool by modulating quinol oxidase activity in thylakoids. J. Bacteriol. , in press.
van de Meene, A.M.L., Hohmann-Marriott, M.F., Vermaas, W.F.J., and Roberson, R.W. (2006) The three-dimensional structure of the cyanobacterium Synechocystis sp. PCC 6803. Arch. Microbiol. 184 , 259-270.
Vavilin, D., Brune , D.C. , and Vermaas, W. (2005) 15 N labeling to determine chlorophyll synthesis and degradation in Synechocystis sp. PCC 6803 strains lacking one or both photosystems. Biochim. Biophys. Acta 1708 , 91-101.
Wenk, S.-O., Schneider, D., Boronowsky, U., Jäger, C., Klughammer, C., de Weerd, F.L., van Roon, H., Vermaas, W.F.J., Dekker, J.P., and Rögner, M. (2005) Functional implications of pigments bound to a cyanobacterial cytochrome b 6 f complex. FEBS J . 272 , 582-592.
Mohamed, H.E., van de Meene, A.M.L., Roberson, R.W., and Vermaas, W.F.J. (2005) Deletion of sll1213 , the fucose synthetase gene in Synechocystis sp. PCC 6803: myxoxanthophyll is required for normal cell wall structure and thylakoid organization in cyanobacteria. J. Bacteriol. 187 , 6883-6892.
Yeremenko, N., Jeanjean, R., Prommeenate, P., Krasikov, V., Nixon, P.J., Vermaas, W.F.J., Havaux, M., and Matthijs, H.C.P. (2005) ORF ssr 2016 encodes a component for Photosystem I driven cyclic electron transfer in the cyanobacterium Synechocystis sp. PCC6803. Plant Cell Physiol. 46 , 1433-1436.
Whitelegge, J.P., Katz, J.E., Pihakari, K.A., Hale, R., Aguilera, R., Gomez, S.M., Faull, K.F., Vavilin, D., and Vermaas, W. (2004) Subtle modification of isotope ratio proteomics: an integrated strategy for expression proteomics. Phytochem. 65 , 1507-1511.
Diner, B.A., Bautista, J.A., Nixon, P.J., Berthomieu, C., Hienerwadel, R., Britt, R.D., Vermaas, W.F.J. , and Chisholm, D.A. (2004) Coordination of proton and electron transfer from the redox-active tyrosine, Y Z , of Photosystem II and examination of the electrostatic influence of oxidized tyrosine, Y D . (H + ). Phys. Chem. Chem. Phys. 6 , 4844-4850.
Xu, H., Vavilin, D., Funk, C., and Vermaas, W. (2004) Small Cab-like proteins in the cyanobacterium Synechocystis sp. PCC 6803 regulate tetrapyrrole biosynthesis: effects of multi-gene deletions. J. Biol. Chem. 279: 27971-27979.
Mohamed, H.E., and Vermaas, W.F.J. ( 2004) Slr1293 in Synechocystis sp. PCC 6803 is the C-3,4 desaturase (CrtD) involved in myxoxanthophyll biosynthesis. J. Bacteriol. 186: 5621-5628.
Vermaas, W.F.J. (2004) Targeted genetic modification of oxygen-producing photosynthetic prokaryotes: New biotechnology applications of ancient organisms. In: Handbook of Microalgal Culture (A. Richmond, ed.), pp. 457-470. Blackwell Science, Oxford.
Kufryk, G.I., and Vermaas, W.F.J. (2003) Functional assignment of new open reading frames in the genome of Synechocystis sp. PCC 6803. In: Molecular Genetics of Marine Organisms (Recent Advances in Marine Biotechnology, Volume 10) (R. Nagabhusanam and M. Fingerman, eds.), pp. 87-122. Science Publishers, Enfield.
Vavilin, D, H Xu, S Lin, and W Vermaas. (2003) Energy and electron transfer in photosystem II of a chlorophyll b-containing Synechocystis sp. PCC 6803 mutant. Biochemistry 42:1731-1746.
Kufryk, GI, and WFJ Vermaas. (2003) Slr2013 is a novel protein regulating folding of the D2 protein of photosystem II in Synechocystis sp. PCC 6803. J. Bacteriol. 185:6615-6623.
Xu, H, D Vavilin, and W Vermaas. (2002) The presence of chlorophyll b in Synechocystis sp. PCC 6803 disturbs tetrapyrrole biosynthesis and enhances chlorophyll degradation. J. Biol. Chem. 277:42726-42732.
Xu, H, D Vavilin, C Funk, and W Vermaas. (2002). Small Cab-like proteins regulating tetrapyrrole biosynthesis in the cyanobacterium Synechocystis sp. PCC 6803. Plant Mol. Biol. 49:149-160.
Berry, S, D Schneider, WFJ Vermaas, and M. Rgner. (2002). Electron transport routes in whole cells of Synechocystis sp. strain PCC 6803: The role of the cytochrome bd-type oxidase. Biochemistry 41:3422-3429.
Kufryk, GI, M Sachet, G Schmetterer, and WFJ Vermaas. (2002). Transformation of the cyanobacterium Synechocystis sp. PCC 6803 as a tool for genetic mapping: optimization of efficiency. FEMS Microbiol. Lett. 206:215-219.
Vavilin, DV and WFJ Vermaas. (2002). Regulation of the tetrapyrrole biosynthetic pathway leading to heme and chlorophyll in plants and cyanobacteria. Physiol. Plant. 115:9-24.
Vermaas, WFJ. (2002). Evolution of photosynthesis. IN: Encyclopedia of Life Sciences http://www.els.net, London: Nature Publishing Group.
Vermaas, WFJ. (2001). Photosynthesis and respiration in cyanobacteria. IN: Encyclopedia of Life Sciences, pp. 245-251. http://www.els.net, London:Nature Publishing Group.
Xu, H, D Vavilin, and W Vermaas. (2001). Chlorophyll b can serve as the major pigment in functional photosystem II complexes of cyanobacteria. Proc. Natl. Acad. Sci. USA 98:14168-14173.
Diner, BA, E Schlodder, PJ Nixon, WJ Coleman, F Rapoport, J Lavergne, WFJ Vermaas, and DAChisholm. (2001). Site-directed mutations at D1-His198 and D2-His197 of photosystem II in Synechocystis PCC 6803: sites of primary charge separation and cation and triplet stabilization. Biochemistry 40:9265-9281.
Howitt, CA, JW Cooley, J Wiskich, and WFJ Vermaas. (2001). A strain of Synechocystis sp. PCC 6803 without photosynthetic oxygen evolution and respiratory oxygen consumption: Implications for the study of cyclic photosynthetic electron transport. Planta 214:46-56.
Kufryk, GI, and WFJ Vermaas. (2001). A novel protein involved in the functional assembly of the oxygen-evolving complex of photosystem II in Synechocystis sp. PCC 6803. Biochemistry 40:9247-9255.
Ermakova-Gerdes, S, Z Yu, and W Vermaas. (2001). Targeted random mutagenesis to identify functionally important residues in the D2 protein of photosystem II in Synechocystis sp. PCC 6803. J Bacteriol 183:145-154.
Keilty, AT, D Vavilin, and WFJ Vermaas. (2001). Functional analysis of combinatorial mutants with changes in the C-terminus of the CD-loop of the D2 protein in photosystem II of Synechocystis sp. PCC 6803. Biochemistry 40:4131-4139.
Cooley, JW, and WFJ Vermaas. (2001). Succinate dehydrogenase and other respiratory pathways in thylakoid membranes of Synechocystis sp. PCC 6803: capacity comparisons and physiological function. J Bacteriol 183:4251-4258.