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Journal of Bacteriology, October 2008, p. 6726-6733, Vol. 190, No. 20
0021-9193/08/$08.00+0     doi:10.1128/JB.01881-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Substrate Specificities and Availability of Fucosyltransferase and β-Carotene Hydroxylase for Myxol 2'-Fucoside Synthesis in Anabaena sp. Strain PCC 7120 Compared with Synechocystis sp. Strain PCC 6803{triangledown} ,{dagger} ,{ddagger}

Mari Mochimaru,1 Hajime Masukawa,2 Takashi Maoka,3 Hatem E. Mohamed,4 Wim F. J. Vermaas,4 and Shinichi Takaichi5*

Department of Natural Sciences, Komazawa University, Tokyo 154-8525, Japan,1 Department of Biological Sciences, Kanagawa University, Hiratsuka 259-1293, Japan,2 Research Institute for Production Development, Kyoto 606-0805, Japan,3 School of Life Sciences, Arizona State University, P.O. Box 874501, Tempe, Arizona 85285-4501,4 Department of Biology, Nippon Medical School, Kawasaki 211-0063, Japan5

Received 29 November 2007/ Accepted 6 August 2008

To elucidate the biosynthetic pathways of carotenoids, especially myxol 2'-glycosides, in cyanobacteria, Anabaena sp. strain PCC 7120 (also known as Nostoc sp. strain PCC 7120) and Synechocystis sp. strain PCC 6803 deletion mutants lacking selected proposed carotenoid biosynthesis enzymes and GDP-fucose synthase (WcaG), which is required for myxol 2'-fucoside production, were analyzed. The carotenoids in these mutants were identified using high-performance liquid chromatography, field desorption mass spectrometry, and 1H nuclear magnetic resonance. The wcaG (all4826) deletion mutant of Anabaena sp. strain PCC 7120 produced myxol 2'-rhamnoside and 4-ketomyxol 2'-rhamnoside as polar carotenoids instead of the myxol 2'-fucoside and 4-ketomyxol 2'-fucoside produced by the wild type. Deletion of the corresponding gene in Synechocystis sp. strain PCC 6803 (sll1213; 79% amino acid sequence identity with the Anabaena sp. strain PCC 7120 gene product) produced free myxol instead of the myxol 2'-dimethyl-fucoside produced by the wild type. Free myxol might correspond to the unknown component observed previously in the same mutant (H. E. Mohamed, A. M. L. van de Meene, R. W. Roberson, and W. F. J. Vermaas, J. Bacteriol. 187:6883-6892, 2005). These results indicate that in Anabaena sp. strain PCC 7120, but not in Synechocystis sp. strain PCC 6803, rhamnose can be substituted for fucose in myxol glycoside. The β-carotene hydroxylase orthologue (CrtR, Alr4009) of Anabaena sp. strain PCC 7120 catalyzed the transformation of deoxymyxol and deoxymyxol 2'-fucoside to myxol and myxol 2'-fucoside, respectively, but not the β-carotene-to-zeaxanthin reaction, whereas CrtR from Synechocystis sp. strain PCC 6803 catalyzed both reactions. Thus, the substrate specificities or substrate availabilities of both fucosyltransferase and CrtR were different in these species. The biosynthetic pathways of carotenoids in Anabaena sp. strain PCC 7120 are discussed.

* Corresponding author. Mailing address: Department of Biology, Nippon Medical School, Kawasaki 211-0063, Japan. Phone: 81 44 733 3584. Fax: 81 44 722 1231. E-mail: takaichi{at}nms.ac.jp

{triangledown} Published ahead of print on 15 August 2008.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

{ddagger} This paper is dedicated to H. Sakurai on the occasion of his 70th birthday.

Journal of Bacteriology, October 2008, p. 6726-6733, Vol. 190, No. 20
0021-9193/08/$08.00+0     doi:10.1128/JB.01881-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Graham, J. E., Bryant, D. A. (2009). The Biosynthetic Pathway for Myxol-2' Fucoside (Myxoxanthophyll) in the Cyanobacterium Synechococcus sp. Strain PCC 7002. J. Bacteriol. 191: 3292-3300 [Abstract] [Full Text]  
  • Makino, T., Harada, H., Ikenaga, H., Matsuda, S., Takaichi, S., Shindo, K., Sandmann, G., Ogata, T., Misawa, N. (2008). Characterization of Cyanobacterial Carotenoid Ketolase CrtW and Hydroxylase CrtR by Complementation Analysis in Escherichia coli. Plant Cell Physiol 49: 1867-1878 [Abstract] [Full Text]  


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