A PKS/NRPS/FAS hybrid gene cluster from Serratia plymuthica RVH1 encoding the biosynthesis of three broad spectrum, zeamine-related antibiotics.

Serratia plymuthica strain RVH1, initially isolated from an industrial food processing environment, displays potent antimicrobial activity towards a broad spectrum of Gram-positive and Gram-negative bacterial pathogens. Isolation and subsequent structure determination of bioactive molecules led to t...

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Autores principales: Joleen Masschelein, Wesley Mattheus, Ling-Jie Gao, Pieter Moons, Rob Van Houdt, Birgit Uytterhoeven, Chris Lamberigts, Eveline Lescrinier, Jef Rozenski, Piet Herdewijn, Abram Aertsen, Chris Michiels, Rob Lavigne
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spelling oai:doaj.org-article:d276ab8c844a4082a283dce5fd4294b92021-11-18T08:01:03ZA PKS/NRPS/FAS hybrid gene cluster from Serratia plymuthica RVH1 encoding the biosynthesis of three broad spectrum, zeamine-related antibiotics.1932-620310.1371/journal.pone.0054143https://doaj.org/article/d276ab8c844a4082a283dce5fd4294b92013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23349809/?tool=EBIhttps://doaj.org/toc/1932-6203Serratia plymuthica strain RVH1, initially isolated from an industrial food processing environment, displays potent antimicrobial activity towards a broad spectrum of Gram-positive and Gram-negative bacterial pathogens. Isolation and subsequent structure determination of bioactive molecules led to the identification of two polyamino antibiotics with the same molecular structure as zeamine and zeamine II as well as a third, closely related analogue, designated zeamine I. The gene cluster encoding the biosynthesis of the zeamine antibiotics was cloned and sequenced and shown to encode FAS, PKS as well as NRPS related enzymes in addition to putative tailoring and export enzymes. Interestingly, several genes show strong homology to the pfa cluster of genes involved in the biosynthesis of long chain polyunsaturated fatty acids in marine bacteria. We postulate that a mixed FAS/PKS and a hybrid NRPS/PKS assembly line each synthesize parts of the backbone that are linked together post-assembly in the case of zeamine and zeamine I. This interaction reflects a unique interplay between secondary lipid and secondary metabolite biosynthesis. Most likely, the zeamine antibiotics are produced as prodrugs that undergo activation in which a nonribosomal peptide sequence is cleaved off.Joleen MasscheleinWesley MattheusLing-Jie GaoPieter MoonsRob Van HoudtBirgit UytterhoevenChris LamberigtsEveline LescrinierJef RozenskiPiet HerdewijnAbram AertsenChris MichielsRob LavignePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 1, p e54143 (2013)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Joleen Masschelein
Wesley Mattheus
Ling-Jie Gao
Pieter Moons
Rob Van Houdt
Birgit Uytterhoeven
Chris Lamberigts
Eveline Lescrinier
Jef Rozenski
Piet Herdewijn
Abram Aertsen
Chris Michiels
Rob Lavigne
A PKS/NRPS/FAS hybrid gene cluster from Serratia plymuthica RVH1 encoding the biosynthesis of three broad spectrum, zeamine-related antibiotics.
description Serratia plymuthica strain RVH1, initially isolated from an industrial food processing environment, displays potent antimicrobial activity towards a broad spectrum of Gram-positive and Gram-negative bacterial pathogens. Isolation and subsequent structure determination of bioactive molecules led to the identification of two polyamino antibiotics with the same molecular structure as zeamine and zeamine II as well as a third, closely related analogue, designated zeamine I. The gene cluster encoding the biosynthesis of the zeamine antibiotics was cloned and sequenced and shown to encode FAS, PKS as well as NRPS related enzymes in addition to putative tailoring and export enzymes. Interestingly, several genes show strong homology to the pfa cluster of genes involved in the biosynthesis of long chain polyunsaturated fatty acids in marine bacteria. We postulate that a mixed FAS/PKS and a hybrid NRPS/PKS assembly line each synthesize parts of the backbone that are linked together post-assembly in the case of zeamine and zeamine I. This interaction reflects a unique interplay between secondary lipid and secondary metabolite biosynthesis. Most likely, the zeamine antibiotics are produced as prodrugs that undergo activation in which a nonribosomal peptide sequence is cleaved off.
format article
author Joleen Masschelein
Wesley Mattheus
Ling-Jie Gao
Pieter Moons
Rob Van Houdt
Birgit Uytterhoeven
Chris Lamberigts
Eveline Lescrinier
Jef Rozenski
Piet Herdewijn
Abram Aertsen
Chris Michiels
Rob Lavigne
author_facet Joleen Masschelein
Wesley Mattheus
Ling-Jie Gao
Pieter Moons
Rob Van Houdt
Birgit Uytterhoeven
Chris Lamberigts
Eveline Lescrinier
Jef Rozenski
Piet Herdewijn
Abram Aertsen
Chris Michiels
Rob Lavigne
author_sort Joleen Masschelein
title A PKS/NRPS/FAS hybrid gene cluster from Serratia plymuthica RVH1 encoding the biosynthesis of three broad spectrum, zeamine-related antibiotics.
title_short A PKS/NRPS/FAS hybrid gene cluster from Serratia plymuthica RVH1 encoding the biosynthesis of three broad spectrum, zeamine-related antibiotics.
title_full A PKS/NRPS/FAS hybrid gene cluster from Serratia plymuthica RVH1 encoding the biosynthesis of three broad spectrum, zeamine-related antibiotics.
title_fullStr A PKS/NRPS/FAS hybrid gene cluster from Serratia plymuthica RVH1 encoding the biosynthesis of three broad spectrum, zeamine-related antibiotics.
title_full_unstemmed A PKS/NRPS/FAS hybrid gene cluster from Serratia plymuthica RVH1 encoding the biosynthesis of three broad spectrum, zeamine-related antibiotics.
title_sort pks/nrps/fas hybrid gene cluster from serratia plymuthica rvh1 encoding the biosynthesis of three broad spectrum, zeamine-related antibiotics.
publisher Public Library of Science (PLoS)
publishDate 2013
url https://doaj.org/article/d276ab8c844a4082a283dce5fd4294b9
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