Proteomics

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Rules of Coexistence: RiPP Recognition Elements Evolved to Prevent Pathway Interference through Leader Peptide Discrimination

ABSTRACT: Identification of the precursor peptide post translational modifications by MALDI-TOF MS followed by Mascot search. LppK kinase modifies conserved Ser3 residue in LppA. LppA peptide fused with N-terminal MBP and C-terminal TrxA mass tag (MW 60.1 kDa) co-expressed with LppB harboring N-terminal Strep-tag and LppK. The LppB-LppA complex was purified using affinity chromatography. Protein zones corresponding to LppA (MBP-LppA-TrxA fused protein, MW 61.5 kDa) were subjected to in-gel digestion with trypsin. The eluted tryptic peptides were identified using MALDI-TOF MS. For the leader peptide cleavage site identification, LppA peptide fused with N-terminal MBP and C-terminal TrxA mass tag (MW 60.1 kDa) co-expressed with LppB harboring N-terminal Strep-tag and LppB2. The LppB-LppA complex was purified using affinity chromatography. Protein zones corresponding to LppA (MBP-LppA-TrxA fused protein, MW 61.5 kDa) were subjected to in-gel digestion with trypsin. The eluted tryptic peptides were identified using MALDI-TOF MS.

ORGANISM(S): Escherichia Coli

SUBMITTER: Svetlana Dubiley 

PROVIDER: PXD070677 | JPOST Repository | Thu Nov 13 00:00:00 GMT 2025

REPOSITORIES: jPOST

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MBP-LppA-Trx%20%20S30%C3%90%C2%90%20.zip Other
MBP-LppA-Trx%20cut.zip Other
MBP-LppA-Trx%20full.zip Other
MBP-LppA-trxA%20S30T%20.zip Other
MBP-LppA-trxA%20S30Y%20.zip Other
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Publications

RiPP recognition elements evolved to prevent pathway interference through leader peptide discrimination.

Popov Aleksandr A   Bikmetov Dmitry D   Grigoreva Anastasiia A   Serebryakova Marina M   Severinov Konstantin K   Wolf Yuri I YI   Lippens Guy G   Wada Akira A   Tagami Shunsuke S   Dubiley Svetlana S  

Nature communications 20260520

Ribosomally synthesized and post-translationally modified peptides (RiPPs) are natural products with diverse structures and functions. Here, we report the discovery of a family of RiPPs whose biosynthetic gene clusters are widespread in the Bacillota genomes and often co-localize with those of lasso peptides, another distinct family of RiPPs. The synthesis of both kinds of RiPPs relies on specific interactions between small adapter protein domains known as RiPP recognition elements (RREs) with t  ...[more]

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