Expression of holo-proteorhodopsin in Synechocystis sp. PCC 6803 |
| |
| Affiliation: | 1. Molecular Microbial Physiology, Swammerdam Institute for Life Sciences, University of Amsterdam, Amsterdam, The Netherlands;2. Mass Spectrometry of Biomacromolecules, Swammerdam Institute for Life Sciences, University of Amsterdam, Amsterdam, The Netherlands;3. Biophysical Organic Chemistry, Leiden Institute of Chemistry, Leiden University, Leiden, The Netherlands;3. Interfaculty Institute for Microbiology and Infection Medicine, Eberhard-Karls University Tübingen, Auf der Morgenstelle 28, 72076 Tübingen, Germany;;4. Plant Biochemistry, Faculty of Biology and Biotechnology, Ruhr University Bochum, Universitätsstraße 150, 44780 Bochum, Germany;;5. Proteome Center Tuebingen, Eberhard-Karls-University Tübingen, Auf der Morgenstelle 15, 72076 Tübingen, Germany;1. Institute for Advanced Materials and Technology, University of Science and Technology Beijing, Beijing, 100083, China;2. Key Laboratory for Corrosion and Protection of the Ministry of Education (MOE), Beijing, 100083, China;3. Beijing Advanced Innovation Center for Materials Genome Engineering, University of Science and Technology Beijing, Beijing, 100083, China;1. MSU-DOE Plant Research Laboratory, Michigan State University, 612 Wilson Road, East Lansing, MI 48824, United States;2. Department of Biochemistry & Molecular Biology, Michigan State University, 603 Wilson Road, East Lansing, MI 48824, United States;1. Laboratory of Synthetic Microbiology, School of Chemical Engineering & Technology, Tianjin University, Tianjin 300072, PR China;2. Key Laboratory of Systems Bioengineering, Ministry of Education of China, Tianjin 300072, PR China;3. Collaborative Innovation Center of Chemical Science and Engineering, Tianjin, PR China;4. Center for Biosafety Research and Strategy, Tianjin University, Tianjin, PR China;1. Key Laboratory of Systems Bioengineering (Ministry of Education), School of Chemical Engineering and Technology, and SynBio Research Platform, Collaborative Innovation Centre of Chemical Science and Engineering, Tianjin University, Tianjin 300072, China;2. Petrochemical Research Institute, PetroChina Company Limited, Beijing 102206, China;3. State Key Laboratory of Marine Resource Utilization in South China Sea, College of Information Science & Technology, Hainan University, Haikou 570228, China;4. State Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China |
| |
| Abstract: | Retinal-based photosynthesis may contribute to the free energy conversion needed for growth of an organism carrying out oxygenic photosynthesis, like a cyanobacterium. After optimization, this may even enhance the overall efficiency of phototrophic growth of such organisms in sustainability applications. As a first step towards this, we here report on functional expression of the archetype proteorhodopsin in Synechocystis sp. PCC 6803. Upon use of the moderate-strength psbA2 promoter, holo-proteorhodopsin is expressed in this cyanobacterium, at a level of up to 105 molecules per cell, presumably in a hexameric quaternary structure, and with approximately equal distribution (on a protein-content basis) over the thylakoid and the cytoplasmic membrane fraction. These results also demonstrate that Synechocystis sp. PCC 6803 has the capacity to synthesize all-trans-retinal. Expressing a substantial amount of a heterologous opsin membrane protein causes a substantial growth retardation Synechocystis, as is clear from a strain expressing PROPS, a non-pumping mutant derivative of proteorhodopsin. Relative to this latter strain, proteorhodopsin expression, however, measurably stimulates its growth. |
| |
| Keywords: | Proton pump All-trans retinal Apo- and holo-protein Proton motive force Thylakoid membrane Cytoplasmic membrane |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
