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Applied and Environmental Microbiology, September 2005, p. 5066-5076, Vol. 71, No. 9
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.9.5066-5076.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Gene Cluster Responsible for Validamycin Biosynthesis in Streptomyces hygroscopicus subsp. jinggangensis 5008

Yi Yu,1 Linquan Bai,1 Kazuyuki Minagawa,2 Xiaohong Jian,1 Lei Li,1 Jialiang Li,1 Shuangya Chen,1 Erhu Cao,1 Taifo Mahmud,2 Heinz G. Floss,3 Xiufen Zhou,1 and Zixin Deng1*

Bio-X Life Science Research Center and School of Life Science & Biotechnology, Shanghai Jiaotong University, Shanghai 200030, People's Republic of China,1 College of Pharmacy, Oregon State University, Corvallis, Oregon 97331-3507,2 Department of Chemistry, University of Washington, Seattle, Washington 98195-17003

Received 3 November 2004/ Accepted 21 March 2005

A gene cluster responsible for the biosynthesis of validamycin, an aminocyclitol antibiotic widely used as a control agent for sheath blight disease of rice plants, was identified from Streptomyces hygroscopicus subsp. jinggangensis 5008 using heterologous probe acbC, a gene involved in the cyclization of D-sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone of the acarbose biosynthetic gene cluster originated from Actinoplanes sp. strain SE50/110. Deletion of a 30-kb DNA fragment from this cluster in the chromosome resulted in loss of validamycin production, confirming a direct involvement of the gene cluster in the biosynthesis of this important plant protectant. A sequenced 6-kb fragment contained valA (an acbC homologue encoding a putative cyclase) as well as two additional complete open reading frames (valB and valC, encoding a putative adenyltransferase and a kinase, respectively), which are organized as an operon. The function of ValA was genetically demonstrated to be essential for validamycin production and biochemically shown to be responsible specifically for the cyclization of D-sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in vitro using the ValA protein heterologously overexpressed in E. coli. The information obtained should pave the way for further detailed analysis of the complete biosynthetic pathway, which would lead to a complete understanding of validamycin biosynthesis.

* Corresponding author. Mailing address: Bio-X Life Science Research Center, Shanghai Jiaotong University, Shanghai 200030, China. Phone: 86 21 62933404. Fax: 86 21 62932418. E-mail: zxdeng{at}sjtu.edu.cn.

Applied and Environmental Microbiology, September 2005, p. 5066-5076, Vol. 71, No. 9
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.9.5066-5076.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.





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