N-terminal acetylation in paenibacillin, a novel lantibiotic

被引：41

作者：

He, Zengguo ^{[1
]}

Yuan, Chunhua ^{[2
]}

Zhang, Liwen ^{[4
]}

Yousef, Ahmed E. ^{[1
,3
]}

机构：

[1] Ohio State Univ, Dept Food Sci & Technol, Columbus, OH 43210 USA

[2] Ohio State Univ, Campus Chem Instrument Ctr, Nucl Magnet Resonance Facil, Columbus, OH 43210 USA

[3] Ohio State Univ, Dept Microbiol, Columbus, OH 43210 USA

[4] Ohio State Univ, Campus Chem Instrument Ctr, Mass Spectrometry & Proteom Facil, Columbus, OH 43210 USA

来源：

FEBS LETTERS | 2008年 / 582卷 / 18期

关键词：

lantibiotics; paenibacillin; NMR; N-terminal acetylation; antibacterial peptides;

D O I：

10.1016/j.febslet.2008.07.008

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

N-terminal acetylation was uncovered in paenibacillin, a novel lantibiotic recently reported as a product of Paenibacillus polymyxa OSY-DF. This N-terminal modi. cation is unprecedented among bacteria-derived antimicrobial peptides and further illustrates the broad range of modi. cations that can occur in lantibiotics. Additionally, the primary structure of paenibacillin has been finally determined unequivocally by the extensive NMR analysis taken together with previous MS/MS results. These analyses revealed the structure of paenibacillin as one of the most post-translationally modified lantibiotics. Published by Elsevier B. V. on behalf of the Federation of European Biochemical Societies.

引用

页码：2787 / 2792

页数：6

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