The role of a conserved threonine residue in the leader peptide of lasso peptide precursors

Pan, Si Jia; Rajniak, Jakub; Maksimov, Mikhail O.; Link, A. James

doi:10.1039/c2cc17211a

Cited by 53 publications

(75 citation statements)

References 27 publications

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“…S1B). Our group has recently investigated the role of threonine in the leader peptides of MccJ25 and capistruin, and found that it is the optimal residue for the production of these peptides in vivo (29,30). Other amino acids similar in size and shape to threonine can be substituted and still lead to efficient production of MccJ25 and capistruin in cells.…”

Section: Resultsmentioning

confidence: 99%

“…3B) consisting of the atxA1, atxB, and atxC genes (NCBI gene IDs 10053804-10053806). There is a 54 base region between the atxA1 and atxB genes that includes an inverted repeat sequence, a feature that has been observed previously in lasso peptide gene clusters (28), including the cluster that codes for capistruin (30). This sequence was removed from the cluster and replaced with a short sequence that includes an optimized E. coli ribosome binding site (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…We cultured A. excentricus in its recommended medium and examined both the culture supernatant and boiled cell lysates for the presence of lasso peptides by MS, but none of the predicted masses were observed. We turned our focus instead to the heterologous production of a single putative lasso peptide in E. coli, a strategy that was successful in the production of capistruin (13,30). The lasso peptide encoded by the atxA1 gene is longer (23 aa) than any known lasso peptide.…”

Section: Resultsmentioning

confidence: 99%

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Precursor-centric genome-mining approach for lasso peptide discovery

Maksimov¹,

Pelczer²,

Link

2012

Proc. Natl. Acad. Sci. U.S.A.

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136

232

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Lasso peptides are a class of ribosomally synthesized posttranslationally modified natural products found in bacteria. Currently known lasso peptides have a diverse set of pharmacologically relevant activities, including inhibition of bacterial growth, receptor antagonism, and enzyme inhibition. The biosynthesis of lasso peptides is specified by a cluster of three genes encoding a precursor protein and two enzymes. Here we develop a unique genome-mining algorithm to identify lasso peptide gene clusters in prokaryotes. Our approach involves pattern matching to a small number of conserved amino acids in precursor proteins, and thus allows for a more global survey of lasso peptide gene clusters than does homology-based genome mining. Of more than 3,000 currently sequenced prokaryotic genomes, we found 76 organisms that are putative lasso peptide producers. These organisms span nine bacterial phyla and an archaeal phylum. To provide validation of the genome-mining method, we focused on a single lasso peptide predicted to be produced by the freshwater bacterium Asticcacaulis excentricus. Heterologous expression of an engineered, minimal gene cluster in Escherichia coli led to the production of a unique lasso peptide, astexin-1. At 23 aa, astexin-1 is the largest lasso peptide isolated to date. It is also highly polar, in contrast to many lasso peptides that are primarily hydrophobic. Astexin-1 has modest antimicrobial activity against its phylogenetic relative Caulobacter crescentus. The solution structure of astexin-1 was determined revealing a unique topology that is stabilized by hydrogen bonding between segments of the peptide.bioinformatics | protein NMR

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Precursor-centric genome-mining approach for lasso peptide discovery

Maksimov¹,

Pelczer²,

Link

2012

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

136

232

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“…68 In particular, the Thr residue in the penultimate position of the leader peptide is proposed to be a recognition element for the maturation enzymes. 314 The final product is believed to be transported from the cytoplasm by an ABC transporter. 284,315 In contrast to microcin J25 and capistruin, which are encoded by four-gene clusters, lariatins A and B, produced by Rhodococcus jostii , result from a five-gene cluster ( larABCDE ).…”

Section: Lasso Peptidesmentioning

confidence: 99%

Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature

et al. 2013

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“…More recently, the era of lasso peptides discovery guided by a genome mining strategy emerged with the characterization of capistruin from Burkholderia thailandensis . Genome mining approaches either protein homology-based Hegemann et al , b, 2014 or precursor-centric (Maksimov et al 2012b) coupled with state-of-the-art detection methods (Kersten et al 2011) proved extremely efficient for lasso peptide discovery, 24 of the 35 currently known lasso peptides being identified by this way. They are mainly from proteobacteria and less frequently from actinobacteria.…”

mentioning

confidence: 99%

Lasso Peptides

Zirah

Rebuffat

2015

SpringerBriefs in Microbiology

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SpringerBriefs in Microbiology present concise summaries of cutting-edge research and practical applications across a wide spectrum of fields. Featuring compact, authored volumes of 50 to 125 pages, the series covers a range of content from professional to academic. Typical topics might include:• A timely report of state-of-the art analytical techniques • A bridge between new research results published in journal articles and a contextual literature review • A snapshot of a hot or emerging topic • An in-depth case study or clinical example • A presentation of core concepts that students must understand in order to make independent contributions • Best practices or protocols to be followed • A series of short case studies SpringerBriefs in Microbiology showcase basic and translational research from a global author community. Briefs allow authors to present their ideas and readers to absorb them with minimal time investment, and will be published as part of Springer's eBook collection, with millions of users worldwide. In addition, Briefs will be available for individual print and electronic purchase.Briefs are characterized by fast, global electronic dissemination, standard publishing contracts, standardized manuscript preparation and formatting guidelines, and expedited production schedules. We aim for publication 8-12 weeks after acceptance.More information about this series at

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The role of a conserved threonine residue in the leader peptide of lasso peptide precursors

Cited by 53 publications

References 27 publications

Precursor-centric genome-mining approach for lasso peptide discovery

Precursor-centric genome-mining approach for lasso peptide discovery

Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature

Lasso Peptides

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