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Journal of Bacteriology, December 2008, p. 7966-7974, Vol. 190, No. 24
0021-9193/08/$08.00+0 doi:10.1128/JB.00985-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.
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Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802
Received 16 July 2008/ Accepted 29 September 2008
The euryhaline, unicellular cyanobacterium Synechococcus sp. strain PCC 7002 produces the dicyclic aromatic carotenoid synechoxanthin (
,
-caroten-18,18'-dioic acid) as a major pigment (>15% of total carotenoid) and when grown to stationary phase also accumulates small amounts of renierapurpurin (
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-carotene) (J. E. Graham, J. T. J. Lecomte, and D. A. Bryant, J. Nat. Prod. 71:1647-1650, 2008). Two genes that were predicted to encode enzymes involved in the biosynthesis of synechoxanthin were identified by comparative genomics, and these genes were insertionally inactivated in Synechococcus sp. strain PCC 7002 to verify their function. The cruE gene (SYNPCC7002_A1248) encodes β-carotene desaturase/methyltransferase, which converts β-carotene to renierapurpurin. The cruH gene (SYNPCC7002_A2246) encodes an enzyme that is minimally responsible for the hydroxylation/oxidation of the C-18 and C-18' methyl groups of renierapurpurin. Based on observed and biochemically characterized intermediates, a complete pathway for synechoxanthin biosynthesis is proposed.
Published ahead of print on 10 October 2008.
Supplemental material for this article may be found at http://jb.asm.org/.
Present address: Center for Marine Biotechnology, University of Maryland Biotechnology Institute, Baltimore, MD 21202.
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