Molecular analysis of the lactacin F operon

Author:

Fremaux C1,Ahn C1,Klaenhammer T R1

Affiliation:

1. Department of Food Science, Southeast Dairy Foods Research Center, North Carolina State University, Raleigh 27695-7624.

Abstract

Lactacin F is a nonlantibiotic, heat-stable, peptide bacteriocin produced by Lactobacillus johnsonii VPI11088. Molecular analysis of the lactacin F DNA region characterized a small operon that codes for three open reading frames, designated lafA, lafX, and ORFZ. The peptide encoded by lafA, the lactacin F structural gene, was compared with various peptide bacteriocins from lactic acid bacteria, and similarities were identified in the amino and carboxy termini of the propeptides. Site-directed mutagenesis of the LafA precursor at the two glycine residues in positions -1 and -2 defined an essential motif for processing of mature lactacin F. The involvement of the peptides encoded by lafX and ORFZ in bacteriocin expression was investigated by subcloning various fragments from the lactacin F region into the shuttle vector pGKV210. In addition to lafA, expression of lafX is essential to lactacin F activity. The lactacin F operon resembles the genetic organization of lactococcin M. Although no function has been assigned to ORFZ by genetic analysis, both peptide Z and the lactococcin M immunity protein are predicted to be integral membrane proteins with four putative transmembrane segments. Lactacin F activity, defined by bactericidal action on Lactobacillus delbrueckii, is dependent on the expression of two genes, lafA and lafX.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

Reference51 articles.

1. Expansion of the bactericidal activity of lactacin F by complementation with a second peptide encoded within the laf operon;Allison G.;FEMS Microbiol. Rev.,1993

2. Detection and activity of lactacin B, a bacteriocin produced by Lactobacillus acidophilus;Barefoot S. F.;Appl. Environ. Microbiol.,1983

3. A membrane-filter technique for the detection of complementary DNA;Denhardt D. T.;Biochem. Biophys. Res. Commun.,1966

4. High efficiency transformation of Eschenchia coli by high voltage electroporation;Dower W. J.;Nucleic Acids Res.,1988

5. Biosynthesis of the lantibiotic nisin: genomic organization and membrane localization of the NisB protein;Engelke G.;Appl. Environ. Microbiol.,1992

Cited by 99 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3