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A B S T R A C T B O O K – A B S T R A C T S O F T A L K S PHOTOSYNTHESIS -PHOTOSYSTEM I IN SYNTHETIC BIOLOGY P. E. Jensen, K. Jensen, L. M. M. Lassen, A. Zygadlo Nielsen, B. L. Møller Department of Plant Biology and Biotechnology, KU-LIFE, Frederiksberg, Copenhagen, Denmark E-mail: peje@life.ku.dk 13 X X I V S P P S C O N G R E S S 2 0 1 1 Invited talk2 Photosystem I (PSI) from plants, algae and cyanobacteria utilizes energy harvested from sunlight to mediate light-driven electron transport across the thylakoid membrane and produce reducing equivalents for the metabolic reactions of the organism. Cytochrome P450s constitute a very large and highly versatile superfamily of membranebound enzymes that catalyse a wide variety of different reactions often difficult to achieve using the approaches of chemical synthesis. In this project we aim at coupling PSI directly to a cytochrome P450 (P450) to develop a system in which the enzymatic reaction of P450s is driven directly by the energy of solar light. In nature, electrons for photosynthetic electron transport are derived from water oxidation at PSII. At PSI, the electrons are donated to ferredoxin (Fd) on the stromal side of the thylakoid membrane. The electrons supplied by PSI may via the soluble electron carrier Fd be donated to ferredoxin NADP + oxidoreductase (FNR), which reduces NADP + to NADPH. In vivo, the electrons required for the reactions of the P450s are taken from NADPH through the NADPH-cytochrome P450 oxidoreductase enzyme. Our recent results demonstrate that the delivery of electrons to the P450 can circumvent the production and oxidation of NADPH, and instead directly transfer electrons from PSI viaFd to an adjacent P450 [1]. A supra-metabolon containing PSI and a cytochrome P450 are being constructed to facilitate highly efficient electron transfer. We aim at linking the P450 enzyme directly to subunits of PSI. Ultimately, the aim is to generate a system in which the fusion protein is stably expressed in the thylakoid membrane of cyanobacteria or plants and utilized to carry out the desired enzymatic reactions in vivo. References [1]Jensen et al., ACS Chem. Biol. 2011
Session <strong>1.</strong> Biotechnology and synthetic biology A B S T R A C T B O O K – A B S T R A C T S O F T A L K S HETEROGONOUS EXPRESSION AND CHARACTERIZATION OF HUMAN MINI- INSULIN PROTEIN IN TOBACCO PLANTS Ji Su Kim, Yu Jin Choi, Ky Young Park Sunchon National University, Jeollanam-do, South Korea E-mail: plpm@sunchon.ac.kr This study is focus on the development for plant-derived biopharmaceuticals using molecular farming by the attempt to propose prototype and search expression system that plant-derived pharmaceutical protein can be produced. The mini-proinsulin is designed by minimizing C-peptide between A and B chain of insulin. Ala-Ala-Lys (AAK) processing site, trypsin cleavage site, is added in the end of Lys residue of B chain and in the front of Gly residue A chain. Also, His6-tag is re-combined to purify insulin in front of a C-terminal ER retention signal (KDEL) sequence which induces protein synthesis with high efficiency by accumulating in the form of protein. Especially, it is made possible to purify insulin protein by one-time trypsin treatment after extraction with His6-tag. Arg(R), Arg(R) dibasic processing site was added between A chain and His6-tag linked with Cpeptide. N. tabacum plants were transformed with this binary expression vector miniinsulinpTRAkt-rfp. After regeneration of transgenic plants in selection medium, the selected transgenic plants (T0) were confirmed the miniinsulin gene by PCR. After purification of miniinsulin protein from transgenic plants (T0), it will be determined whether it has an accurate molecular weight and processing, and then it has a physiological activity for insulin in vitro. 14 X X I V S P P S C O N G R E S S 2 0 1 1
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Page 3 and 4: Foreword eword ord A B S T R A C T
Page 5 and 6: Program of the Congress gram of the
Page 7 and 8: A B S T R A C T B O O K - P R O G R
Page 9 and 10: A B S T R A C T B O O K - P R O G R
Page 11 and 12: Plenary session 1 A B S T R A C T B
Page 13: Plenary session 2 THE BIOLOGY OF AL
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Page 19 and 20: Session 2. Systems biology and -omi
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Page 27 and 28: Pleanary session 4 A B S T R A C T
Page 29 and 30: Invited talk 4 A B S T R A C T B O
Page 31 and 32: Session 5.Cell biology A B S T R A
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Page 37 and 38: Session 7.Development A B S T R A C
Page 39 and 40: Session 8.Signalling A B S T R A C
Page 41 and 42: Pleanary session 6 A B S T R A C T
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A B S T R A C T B O O K - A B S T R
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Sapporo Medical University, Sapporo
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SCF = A B S T R A C T B O O K - A B
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A B S T R A C T B O O K - L I S T O
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A B S T R A C T B O O K - L I S T O
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Sponsors onsors ors A B S T R A C T
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