Bioengineering of lanthipeptides in Escherichia coli: assessing the specificity of lichenicidin and haloduracin biosynthetic machinery

被引：13

作者：

Caetano, T. ^{[1
,2
]}

Barbosa, J. ^{[1
,2
]}

Moeesker, E. ^{[3
]}

Suessmuth, R. D. ^{[3
]}

Mendo, S. ^{[1
,2
]}

机构：

[1] Univ Aveiro, Dept Biol, P-3810 Aveiro, Portugal

[2] Univ Aveiro, CESAM, P-3810 Aveiro, Portugal

[3] Tech Univ Berlin, Inst Chem, D-10623 Berlin, Germany

来源：

RESEARCH IN MICROBIOLOGY | 2014年 / 165卷 / 07期

关键词：

Bacillus; Bacteriocins; Chimeras; In vivo; Lantibiotics; HETEROLOGOUS EXPRESSION; LACTICIN-481; SYNTHETASE; BACILLUS-LICHENIFORMIS; LEADER SEQUENCE; AMINO-ACIDS; PEPTIDE; LANTIBIOTICS; NISIN; DISCOVERY;

D O I：

10.1016/j.resmic.2014.07.006

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The lichenicidin and haloduracin biosynthetic machinery specificity was investigated in vivo in Escherichia coli. Unlike previous reports using different hosts, it was found that the biosynthetic machineries of lichenicidin and haloduracin are highly specific to their dedicated peptide precursors. Likewise, the substitution of lichenicidin structural genes by chimeras of lichenicidin leader sequences and haloduracin core peptides did not yield mature haloduracin peptides. Despite these restrictions, it was found that the bifunctional enzyme HalT was able to process and export lichenicidin peptides. These findings corroborate the promiscuity of LanT enzymes reported for other lantibiotics, such as nukacin ISK-1 and lacticin 481. (C) 2014 Institut Pasteur. Published by Elsevier Masson SAS. All rights reserved.

引用

页码：600 / 604

页数：5

共 25 条

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