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Journal of Bacteriology, September 2000, p. 5262-5266, Vol. 182, No. 18
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Lantibiotic Biosynthesis: Interactions between Prelacticin 481 and Its Putative Modification Enzyme, LctM

Patricia Uguen, Jean-Paul Le Pennec, and Alain Dufour^*

Laboratoire de Biologie et Chimie Moléculaires, EA 2594, Université de Bretagne Sud, Vannes, France

Received 14 April 2000/Accepted 21 June 2000

Class AII and AIII lantibiotics and mersacidin are antibacterial peptides containing unusual residues obtained by posttranslational modifications of prepeptides, presumably catalyzed by LanM. LctM, the LanM for lacticin 481, is essential for the production of this class AII lantibiotic. Using the yeast two-hybrid system, we showed direct contact between the prelacticin 481 and LctM, supporting the proposed LctM function. Sixteen domains are conserved between the 10 known LanM proteins, whereas three additional domains were found only in class AII LanM proteins and in MrsM, the LanM for mersacidin. All the truncated LctM proteins that we tested presented impaired LctA-binding activity.

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^* Corresponding author. Mailing address: LBCM, UBS, Avenue de Tohannic, 56000 Vannes, France. Phone: (33) 2-97-68-31-93. Fax: (33) 2-97-68-16-39. E-mail: alain.dufour{at}univ-ubs.fr.

Present address: Chemical Pathology Unit, Sir William Dunn School of Pathology, Oxford OX1 3RE, United Kingdom.

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Journal of Bacteriology, September 2000, p. 5262-5266, Vol. 182, No. 18
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

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