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Article

verA Gene is Involved in the Step to Make the Xanthone Structure of Demethylsterigmatocystin in Aflatoxin Biosynthesis

1
Food Research Institute, National Agriculture and Food Research Organization (NARO), 2-1-12 Kannon-dai, Tsukuba-shi 305-8642, Ibaraki, Japan
2
Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, China
3
Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China
4
Faculty of Agriculture, Tottori University, Koyama, Tottori 680-8553, Japan
5
Department of Applied Chemistry and Food Science, Faculty of Environmental and Information Sciences, Fukui University of Technology, 3-6-1 Gakuen, Fukui-shi, Fukui 910-8505, Japan
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(17), 6389; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21176389
Received: 26 July 2020 / Revised: 22 August 2020 / Accepted: 26 August 2020 / Published: 2 September 2020
(This article belongs to the Special Issue Molecular Biology and Chemistry of Mycotoxins and Phytotoxins)
In the biosynthesis of aflatoxin, verA, ver-1, ordB, and hypA genes of the aflatoxin gene cluster are involved in the pathway from versicolorin A (VA) to demethylsterigmatocystin (DMST). We herein isolated each disruptant of these four genes to determine their functions in more detail. Disruptants of ver-1, ordB, and hypA genes commonly accumulated VA in their mycelia. In contrast, the verA gene disruptant accumulated a novel yellow fluorescent substance (which we named HAMA) in the mycelia as well as culture medium. Feeding HAMA to the other disruptants commonly caused the production of aflatoxins B1 (AFB1) and G1 (AFG1). These results indicate that HAMA pigment is a novel aflatoxin precursor which is involved at a certain step after those of ver-1, ordB, and hypA genes between VA and DMST. HAMA was found to be an unstable substance to easily convert to DMST and sterigmatin. A liquid chromatography-mass spectrometry (LC-MS) analysis showed that the molecular mass of HAMA was 374, and HAMA gave two close major peaks in the LC chromatogram in some LC conditions. We suggest that these peaks correspond to the two conformers of HAMA; one of them would be selectively bound on the substrate binding site of VerA enzyme and then converted to DMST. VerA enzyme may work as a key enzyme in the creation of the xanthone structure of DMST from HAMA. View Full-Text
Keywords: aflatoxin biosynthesis; enzyme gene; dmtA (aflO); hypA (aflY); ordB (aflX); HAMA intermediate; stcP; verA (aflN); ver-1 (aflM) aflatoxin biosynthesis; enzyme gene; dmtA (aflO); hypA (aflY); ordB (aflX); HAMA intermediate; stcP; verA (aflN); ver-1 (aflM)
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MDPI and ACS Style

Zeng, H.; Cai, J.; Hatabayashi, H.; Nakagawa, H.; Nakajima, H.; Yabe, K. verA Gene is Involved in the Step to Make the Xanthone Structure of Demethylsterigmatocystin in Aflatoxin Biosynthesis. Int. J. Mol. Sci. 2020, 21, 6389. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21176389

AMA Style

Zeng H, Cai J, Hatabayashi H, Nakagawa H, Nakajima H, Yabe K. verA Gene is Involved in the Step to Make the Xanthone Structure of Demethylsterigmatocystin in Aflatoxin Biosynthesis. International Journal of Molecular Sciences. 2020; 21(17):6389. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21176389

Chicago/Turabian Style

Zeng, Hongmei, Jingjing Cai, Hidemi Hatabayashi, Hiroyuki Nakagawa, Hiromitsu Nakajima, and Kimiko Yabe. 2020. "verA Gene is Involved in the Step to Make the Xanthone Structure of Demethylsterigmatocystin in Aflatoxin Biosynthesis" International Journal of Molecular Sciences 21, no. 17: 6389. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21176389

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