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Unusual Class I Lanthipeptides from the Marine Bacteria Thalassomonas viridans.

ABSTRACT: A novel class I lanthipeptide produced by the marine bacterium Thalassomonas viridans XOM25^T was identified using genome mining. The putative lanthipeptides were heterologously coexpressed in Escherichia coli as GFP-prepeptide fusions along with the operon-encoded class I lanthipeptide modification machinery VdsCB. The core peptides, VdsA1 and VdsA2, were liberated from GFP using the NisP protease, purified, and analyzed by collision-induced tandem mass spectrometry. The operon-encoded cyclase and dehydratase, VdsCB, exhibited lanthipeptide synthetase activity via post-translational modification of the VdsA1 and VdsA2 core peptides. Modifications were directed by the conserved double glycine leader containing prepeptides of VdsA1 and VdsA2.

SUBMITTER: Vermeulen R

PROVIDER: S-EPMC9680876 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature

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Unusual Class I Lanthipeptides from the Marine Bacteria Thalassomonas viridans.

Vermeulen Ross R Van Staden Anton Du Preez ADP van Zyl Leonardo Joaquim LJ Dicks Leon M T LMT Trindade Marla M

ACS synthetic biology 20221102 11

A novel class I lanthipeptide produced by the marine bacterium Thalassomonas viridans XOM25T was identified using genome mining. The putative lanthipeptides were heterologously coexpressed in Escherichia coli as GFP-prepeptide fusions along with the operon-encoded class I lanthipeptide modification machinery VdsCB. The core peptides, VdsA1 and VdsA2, were liberated from GFP using the NisP protease, purified, and analyzed by collision-induced tandem mass spectrometry. The ...[more]

PMID: 36323319

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