Discovery and characterization of a novel C-terminal peptide carboxyl methyltransferase in a lassomycin-like lasso peptide biosynthetic pathway

Su, Yu; Han, Meng; Meng, Xianbin; Feng, Yue; Luo, Shi-Zhong; Chen, Yu; Zheng, Guojun; Zhu, Shaozhou

doi:10.1007/s00253-019-09645-x

Cited by 21 publications

(31 citation statements)

References 60 publications

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“…Post-translational modifications are unusual in lasso peptides, although a few examples have been reported recently, including the C-terminal phosphorylation in paeninodin [27], citrullination in citrulassin A [14], acetylation in albusnodin [28], C-terminal methylation of lassomycin and lassomycin-like lasso peptides [29,30], and the epimerization of the α-carbon from the C-terminal amino acid residue in MS-271 [31]. In this work, we prove that resACB1B2EFD, identified through a genome-mining approach, is sufficient for the biosynthesis of the lasso peptide RES-701-3 and its 7hydroxy-tryptophan homologue RES-701-4 employing Streptomyces coelicolor M1152 and M1154 as On the other hand, no production of either RES-701-3 or RES-701-4 could be detected in any of the exconjugant J1074-pCAPRES clones employed under any of the growth conditions used.…”

Section: Discussionmentioning

confidence: 99%

Identification, Cloning and Heterologous Expression of the Gene Cluster Directing RES-701-3, -4 Lasso Peptides Biosynthesis from a Marine Streptomyces Strain

et al. 2020

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RES-701-3 and RES-701-4 are two class II lasso peptides originally identified in the fermentation broth of Streptomyces sp. RE-896, which have been described as selective endothelin type B receptor antagonists. These two lasso peptides only differ in the identity of the C-terminal residue (tryptophan in RES-701-3, 7-hydroxy-tryptophan in RES-701-4), thus raising an intriguing question about the mechanism behind the modification of the tryptophan residue. In this study, we describe the identification of their biosynthetic gene cluster through the genome mining of the marine actinomycete Streptomyces caniferus CA-271066, its cloning and heterologous expression, and show that the seven open reading frames (ORFs) encoded within the gene cluster are sufficient for the biosynthesis of both lasso peptides. We propose that ResE, a protein lacking known putatively conserved domains, is likely to play a key role in the post-translational modification of the C-terminal tryptophan of RES-701-3 that affords RES-701-4. A BLASTP search with the ResE amino acid sequence shows the presence of homologues of this protein in the genomes of eight other Streptomyces strains, which also harbour the genes encoding the RES-701-3, -4 precursor peptide, split-B proteins and ATP-dependent lactam synthetase required for the biosynthesis of these compounds.

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Section: Discussionmentioning

confidence: 99%

Identification, Cloning and Heterologous Expression of the Gene Cluster Directing RES-701-3, -4 Lasso Peptides Biosynthesis from a Marine Streptomyces Strain

et al. 2020

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“…2013a,b, 2014; Maksimov and Link, 2013;Zimmermann et al, 2013, 2014Metelev et al, 2015Zhao et al, 2016;Su et al, 2019). Notably, the E-B fusion occurs only in a subset of Proteobacteria, while discrete E and B proteins are found in Firmicutes and Actinobacteria.…”

Section: Figure 2 | (A)mentioning

confidence: 99%

“…Heterologous expression is a useful tool for the production of poorly expressed or silent lasso peptide biosynthetic gene clusters. For example, astexin-1 is not detected in Asticcacaulis excentricus under laboratory conditions, while FIGURE 3 | Organization of commonly known lasso peptides from Actinobacteria, Proteobacteria, and Firmicutes (Solbiati et al, 1999;Knappe et al, 2008;Inokoshi et al, 2012;Maksimov et al, 2012b;Hegemann et al, 2013bHegemann et al, , 2014Maksimov and Link, 2013;Zimmermann et al, 2014;Zhu et al, 2016a;Kodani et al, 2018;Su et al, 2019;Yu et al, 2020).…”

Section: Heterologous Expression Of Lasso Peptidesmentioning

confidence: 99%

“…Lassomycin exhibits remarkable activity against multidrug-resistant M. tuberculosis. The bactericidal mechanism of lassomycin stimulates the ATPase activity of ClpC1 but uncouples it from ClpP1P2-dependent proteolysis (Su et al, 2019). Lariatin A/B also shows notable anti-TB activity by targeting M. tuberculosis cells (Zhu et al, 2019).…”

Section: Potential Application Of Lasso Peptides Therapeutical Potentmentioning

confidence: 99%

“…Also, the libraries of lasso peptide heterologous expression systems including synthesis methods and producing strains need to be significantly expanded. Despite extensive experimental and computational studies of lasso peptides (Hegemann et al, 2015;Tietz et al, 2017;Su et al, 2019), the regulation of the production of lasso peptides and deciphering the roles of lasso peptides in nature are great challenges for the next years.…”

Section: Conclusion and Prospectsmentioning

confidence: 99%

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Lasso Peptides: Heterologous Production and Potential Medical Application

Cheng

Hua

2020

Front. Bioeng. Biotechnol.

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Lasso peptides are natural products found in bacteria. They belong to a specific family of ribosomally-synthesized and posttranslationally-modified peptides with an unusual lasso structure. Lasso peptides possess remarkable thermal and proteolytic stability and various biological activities, such as antimicrobial activity, enzyme inhibition, receptor blocking, anticancer properties and HIV antagonism. They have promising potential therapeutic effects on gastrointestinal diseases, tuberculosis, Alzheimer's disease, cardiovascular disease, fungal infections and cancer. Lasso peptides with high stability have been shown to be good carriers for other bioactive peptides. These make them attractive candidates for pharmaceutical research. This review aimed to describe the strategies used for the heterologous production of lasso peptides. Also, it indicated their therapeutical potential and their capacity to use as an efficient scaffold for epitope grafting.

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Advances in screening, synthesis, modification, and biomedical applications of peptides and peptide aptamers

Liu,

Lu,

Chen

et al. 2023

BioFactors

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Peptides and peptide aptamers have emerged as promising molecules for a wide range of biomedical applications due to their unique properties and versatile functionalities. The screening strategies for identifying peptides and peptide aptamers with desired properties are discussed, including high‐throughput screening, display screening technology, and in silico design approaches. The synthesis methods for the efficient production of peptides and peptide aptamers, such as solid‐phase peptide synthesis and biosynthesis technology, are described, along with their advantages and limitations. Moreover, various modification techniques are explored to enhance the stability, specificity, and pharmacokinetic properties of peptides and peptide aptamers. This includes chemical modifications, enzymatic modifications, biomodifications, genetic engineering modifications, and physical modifications. Furthermore, the review highlights the diverse biomedical applications of peptides and peptide aptamers, including targeted drug delivery, diagnostics, and therapeutic. This review provides valuable insights into the advancements in screening, synthesis, modification, and biomedical applications of peptides and peptide aptamers. A comprehensive understanding of these aspects will aid researchers in the development of novel peptide‐based therapeutics and diagnostic tools for various biomedical challenges.

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Discovery and characterization of a novel C-terminal peptide carboxyl methyltransferase in a lassomycin-like lasso peptide biosynthetic pathway

Cited by 21 publications

References 60 publications

Identification, Cloning and Heterologous Expression of the Gene Cluster Directing RES-701-3, -4 Lasso Peptides Biosynthesis from a Marine Streptomyces Strain

Identification, Cloning and Heterologous Expression of the Gene Cluster Directing RES-701-3, -4 Lasso Peptides Biosynthesis from a Marine Streptomyces Strain

Lasso Peptides: Heterologous Production and Potential Medical Application

Advances in screening, synthesis, modification, and biomedical applications of peptides and peptide aptamers

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