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Robert L. Burnap |  |
| Oklahoma State University | ||
 Professor,
Department of Microbiology and Molecular Genetics |
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| Address:
307 Life Sciences
East, OSU, Stillwater, OK 74078
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| Phone:
405-744-7445
Fax: 405-744-6790
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| Email:
burnap@biochem.okstate.edu |
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| URL:
http://microbiology.okstate.edu/faculty/burnap/ |
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| Ph.D.,
Cell Biology, 1987, University
of California Santa Barbara |
Lab Photo | |
| Postdoctoral: Molecular
Genetics and Biophysics of Photosynthesis 1987-91, Purdue University
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| Research
Emphasis: Molecular
analysis of photosynthesis; Functional genomics of ion homeostasis and stress tolerance in cyanobacteria |
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| Related
Activities: |
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| Research
Description: Assembly and function of the cyanobacterial H2O-oxidation complex This project is primarily aimed at understanding the assembly of the multinuclear manganese cluster of the photosystem II complex. It is a particularly fascinating metalloprotein assembly problem since it involves an ordered multi-step sequence of metal ion binding and protein rearrangement. The events include light-initiated metal ion binding events that occur in the microsecond time domain and trigger intervening protein rearrangements occurring the tens of millisecond time domain. The principal objectives of the project are to define these intermediates in terms of kinetics and structural states. Experimental approaches include polarographic, spectroscopic , and cysteine-scanning /chemical modification techniques. NSF Multiuser Cyanobacterial Resource: Whole genome DNA Microarrays The goal of this project is to utilize the Synechocystis sp. PCC6803 genomic sequence to develop DNA microarrays, thus enabling efficient techniques to monitor global patterns of differential transcription in this important model system. The project is producing and utilizing a PCR-generated gene set representing the entire 3168 genes of the Synechocystis sp. PCC6803 genome, a unicellular, transformable cyanobacterium that is an important model organism for the study of photosynthesis and environmental gene regulation. The effort will augment the ability, for example, to follow the transcriptional changes accompanying assembly and re-synthesis of photosystem II complex which has a high turn-over rate due to inherent and frequent photodamage events accompanying its enzymatic activity. The ability to generate and maintain ion gradients across cellular membranes is fundamental to all living organisms. It forms the basis for phenomenon as diverse as nutrient uptake and energy transduction to kidney and nerve function. Ion transport is generally a highly dynamic and energy demanding process. In cyanobacteria, as much as 1/3 of the energy yielded by photosynthesis is expended towards the transmembrane movement of ions, notably the extrusion of sodium. The flux of sodium through the cytoplasmic membrane is strongly light-dependent and is coupled to the movement of other ions, including the uptake of bicarbonate and other nutrients. The long-term goal of this project is to elucidate the molecular mechanisms that maintain ion homeostasis and how these mechanisms are integrated with electron and proton fluxes associated with oxygenic photosynthesis and respiration. Despite its importance, ion homeostasis in cyanobacteria, remains poorly understood. The proposed work will address important questions regarding the transport and regulation of the critical coupling ions, Na+ and H+. Our prokaryotic experimental model, Synechocystis is an ideal model for stress responses in a simple autotroph - photosynthesis, ROS scavenging, respiration and chloroplast functions. The organism can be transformed with very high efficiency relying on homologous recombination. This cyanobacterial genome, 3.6 Mb, is completely sequenced , and the small, non-redundant genome allows precise chromosome engineering including rapid PCR-mediated techniques . |
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| Recent
Publications: Wang HL, Postier B, Burnap RL (2003) Alterations in global patterns of gene expression in Synechocystis sp. PCC 6803 in response to inorganic carbon limitation and the inactivation of ndhR, a LysR family regulator. J Biological Chemistry (in press). Postier B, Wang HL, Singh A, Impson L, Andrews H, Klahn J, Risinger G, Pesta D, Deyholos M, Galbraith D, Sherman LA, Burnap RL (2003) The construction and use of bacterial DNA microarrays based on an optimized two-stage PCR strategy. BMC Genomics 4(1):23. Wang HL, Postier BL, Burnap
RL (2002) Optimization of fusion PCR for in vitro construction of
gene knock-out fragments. Biotechniques 33:26-32. |
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| Selected
Additional Publications: Li Z-L, Burnap RL (2001) Mutations of the strictly conserved arginine 64 within the putative Ca2+-binding lumenal interhelical a-b loop of the Photosystem II D1 protein on the kinetics of photoactivation and H2O-oxidation in Synechocystis sp. PCC6803. Biochemistry 40: 10350-10359. Debus RJ, Gregor W, Campbell KA, Li Z-L, Burnap RL, Britt RD (2001) Does histidine 332 of the D1 polypeptide ligate the manganese cluster in photosystem II? An electron spin echo envelope modulation study. Biochemistry 40: 3690-3699. Bohnert H, Borchert ., Bressan RA, Burnap RL, Cushman JC, Cushman MA, Deyholos M, Galbraith DW, Hasegawa PM, Kawasaki S, Koiwa H, Kore-eda S, Lee B-H, Michalowski CB, Nomura M, Prade R, Tanaka Y, Wang H, Zhu JK A (2000) Genomics approach towards salt stress tolerance: Consortium "Functional Genomics of Plant Stress Tolerance" Plant Physiol Biochem 39:1-17. Li Z-L, Bricker TM, Burnap RL (2000) Kinetic characterization of His-tagged CP47 Photosystem II in Synechocystis sp. PCC6803 Biochim. Biophys Acta 1460:384-389. Al-Khaldi S, Coker J, Shen, J-R, Burnap RL (2000) Characterization of site-directed mutations in the manganese-stabilizing protein of Synechocystis sp. PCC6803 unable to grow photoautotrophically in the absence of cytochrome c-550. Plant Mol Biol 43:33-41. |
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