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Applied and Environmental Microbiology, September 2001, p. 4105-4110, Vol. 67, No. 9
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.9.4105-4110.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

gly Gene Cloning and Expression and Purification of Glycinecin A, a Bacteriocin Produced by Xanthomonas campestris pv. glycines 8ra

Sunggi Heu,1,dagger Jonghee Oh,2 Youngsung Kang,2 Sangryeol Ryu,2 Somi K. Cho,3 Youngsup Cho,1 and Moonjae Cho4,*

Department of Agricultural Biology1 and School of Agricultural Biotechnology,2 College of Agriculture and Life Sciences, Seoul National University, Suwon 441-744, Kumho Life and Environmental Science Laboratory, Kwangju 500-712,3 and Department of Medicine, Cheju National University Medical School, Jeju 690-756,4 Korea

Received 2 April 2001/Accepted 20 June 2001

Glycinecin A, a bacteriocin produced by Xanthomonas campestris pv. glycines, inhibits the growth of X. campestris pv. vesicatoria. We have cloned and expressed the genes encoding glycinecin A in Escherichia coli. Recombinant glycinecin A was purified from cell extracts by ammonium sulfate precipitation followed by chromatography on Q-Sepharose, Mono Q (ion exchange), and size exclusion columns. Purified glycinecin A is composed of two polypeptides, is active over a wide pH range (6 to 9), and is stable at temperatures up to 60°C. Glycinecin A is a heterodimer consisting of 39- and 14-kDa subunits, as revealed through size exclusion chromatography and cross-linking analysis. Two genes, glyA and glyB, encoding the 39- and 14-kDa subunits, respectively, were identified based on the N-terminal sequences of the subunits. From the nucleotide sequences of glyA and glyB, we conclude that both genes are translated as bacteriocin precursors that include N-terminal leader sequences. When expressed in E. coli, recombinant glycinecin A was found primarily in cell extracts. In contrast, most glycinecin A from Xanthomonas was found in the culture media. E. coli transformed with either glyA or glyB separately did not show the bacteriocin activity.

* Corresponding author. Mailing address: Department of Biochemistry, Cheju National University Medical School, Ara-1, Jeju 690-756, Korea. Phone: 82-64-754-3837. Fax: 82-64-725-2593. E-mail: moonjcho{at}cheju.cheju.ac.kr.

dagger Present address: Department of Molecular Genetics, NIAST, RDA, Suwon 441-707, Korea.

Applied and Environmental Microbiology, September 2001, p. 4105-4110, Vol. 67, No. 9
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.9.4105-4110.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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