2-epi-5-epi-Valiolone synthase activity is essential for maintaining phycobilisome composition in the cyanobacterium Anabaena variabilis ATCC 29413 when grown in the p
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- 作者：Edward Spence (1)
Samantha J. Bryan (2)
Mohamed Lisfi (3)
John Cullum (3)
Walter C. Dunlap (1) (4)
J. Malcolm Shick (5)
Conrad W. Mullineaux (2)
Paul F. Long (1) (6) - 关键词：Fructose ; Pentose phosphate pathway ; Phycobilisome ; Phycocyanin ; Mycosporine ; like amino acids ; Sedoheptulose 7 ; phosphate
- 刊名：Photosynthesis Research
- 出版年：2013
- 出版时间：September 2013
- 年：2013
- 卷：116
- 期：1
- 页码：33-43
- 全文大小：693KB
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Samantha J. Bryan (2)
Mohamed Lisfi (3)
John Cullum (3)
Walter C. Dunlap (1) (4)
J. Malcolm Shick (5)
Conrad W. Mullineaux (2)
Paul F. Long (1) (6)
1. Institute of Pharmaceutical Science, King鈥檚 College London, 150 Stamford Street, London, SE1 9NH, UK
2. The School of Biological and Chemical Sciences, Queen Mary University of London, Mile End Road, London, E1 4NS, UK
3. Department of Genetics, University of Kaiserslautern, Postfach 3049, 67653, Kaiserslautern, Germany
4. Centre for Marine Microbiology and Genetics, Australian Institute of Marine Science, Townsville, QLD, 4810, Australia
5. School of Marine Sciences, University of Maine, 5751, Murray Hall, Orono, ME, 04469-5751, USA
6. Department of Chemistry, King鈥檚 College London, 150 Stamford Street, London, SE1 9NH, UK - ISSN：1573-5079
文摘
The cyclase 2-epi-5-epi-valiolone synthase (EVS) is reported to be a key enzyme for biosynthesis of the mycosporine-like amino acid shinorine in the cyanobacterium Anabaena variabilis ATCC 29413. Subsequently, we demonstrated that an in-frame complete deletion of the EVS gene had little effect on in vivo production of shinorine. Complete segregation of the EVS gene deletion mutant proved difficult and was achieved only when the mutant was grown in the dark and in a medium supplemented with fructose. The segregated mutant showed a striking colour change from native blue-green to pale yellow-green, corresponding to substantial loss of the photosynthetic pigment phycocyanin, as evinced by combinations of absorbance and emission spectra. Transcriptional analysis of the mutant grown in the presence of fructose under dark or light conditions revealed downregulation of the cpcA gene that encodes the alpha subunit of phycocyanin, whereas the gene encoding nblA, a protease chaperone essential for phycobilisome degradation, was not expressed. We propose that the substrate of EVS (sedoheptulose 7-phosphate) or possibly lack of its EVS-downstream products, represses transcription of cpcA to exert a hitherto unknown control over photosynthesis in this cyanobacterium. The significance of this finding is enhanced by phylogenetic analyses revealing horizontal gene transfer of the EVS gene of cyanobacteria to fungi and dinoflagellates. It is also conceivable that the EVS gene has been transferred from dinoflagellates, as evident in the host genome of symbiotic corals. A role of EVS in regulating sedoheptulose 7-phosphate concentrations in the photophysiology of coral symbiosis is yet to be determined.