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Sebastian W Fuchs, Gerald Lackner, Brandon I Morinaka, Yohei Morishita, Teigo Asai, Sereina Riniker, Jörn Piel
Ribosomally synthesized and posttranslationally modified peptide natural products (RiPPs) exhibit diverse structures and bioactivities and are classified into distinct biosynthetic families. A recently reported family is the proteusins, with the prototype members polytheonamides being generated by almost 50 maturation steps, including introduction of d-residues at multiple positions by an unusual radical SAM epimerase. A region in the protein-like N-terminal leader of proteusin precursors is identified that is crucial for epimerization...
September 26, 2016: Angewandte Chemie
Tianlu Mo, Lingui Xue, Qi Zhang
Lanthipeptides are a growing class of ribosomally synthesized and posttranslationally modified peptide (RiPP) natural products. These compounds are widely distributed among taxonomically distant species, and their structures and biological activities are diverse, providing an important source for drug research and developement. In this review, we summarized the recent advances in the understanding of structure, classification, evolution and substrate-controlled biosynthetic mechanism of lanthipeptide, attempting to highlight the intriguing chemistry and enzymology in the biosynthesis of this growing family of natural products...
March 4, 2016: Wei Sheng Wu Xue Bao, Acta Microbiologica Sinica
Weixin Tang, Gabrielle N Thibodeaux, Wilfred A van der Donk
Stereochemical control is critical in natural product biosynthesis. For ribosomally synthesized and post-translationally modified peptides (RiPPs), the mechanism(s) by which stereoselectivity is achieved is still poorly understood. In this work, we focused on the stereoselective lanthionine synthesis in lanthipeptides, a major class of RiPPs formed by the addition of Cys residues to dehydroalanine (Dha) or dehydrobutyrine (Dhb). Nonenzymatic cyclization of the small subunit of a virulence lanthipeptide, the enterococcal cytolysin, resulted in the native modified peptide as the major product, suggesting that both regioselectivity and stereoselectivity are inherent to the dehydrated peptide sequence...
September 16, 2016: ACS Chemical Biology
Elvis Legala Ongey, Peter Neubauer
Lanthipeptides (also called lantibiotics for those with antibacterial activities) are ribosomally synthesized post-translationally modified peptides having thioether cross-linked amino acids, lanthionines, as a structural element. Lanthipeptides have conceivable potentials to be used as therapeutics, however, the lack of stable, high-yield, well-characterized processes for their sustainable production limit their availability for clinical studies and further pharmaceutical commercialization. Though many reviews have discussed the various techniques that are currently employed to produce lanthipeptides, a direct comparison between these methods to assess industrial applicability has not yet been described...
2016: Microbial Cell Factories
Hongwei Liu, Shuli Yin, Likang An, Genwei Zhang, Huicai Cheng, Yanhua Xi, Guanhui Cui, Feiyan Zhang, Liping Zhang
Bacillus subtilis BSD-2, isolated from cotton (Gossypium spp.), had strong antagonistic activity to Verticillium dahlia Kleb and Botrytis cinerea. We sequenced and annotated the BSD-2 complete genome to help us the better use of this strain, which has surfactin, bacilysin, bacillibactin, subtilosin A, Tas A and a potential class IV lanthipeptide biosynthetic pathways.
July 20, 2016: Journal of Biotechnology
Neha Garg, Yuki Goto, Ting Chen, Wilfred A van der Donk
The biosynthesis of the class II lanthipeptide geobacillin II was reconstituted in vitro. The purified precursor peptide was modified by the lanthipeptide synthetase GeoM at temperatures ranging between 37 °C and 80 °C demonstrating the thermostability of the enzyme. Geobacillin II shares with cytolysin, haloduracin, and carnolysin a DhxDhxXxxXxxCys motif (Dhx =dehydroalanine or dehydrobutyrine) as precursor to its N-terminal A-ring. Like in these other three lantibiotics, the lanthionine in the A-ring of geobacillin II had the LL stereochemical configuration as shown by chiral gas chromatography/mass spectrometry...
May 14, 2016: Biopolymers
Dikla Aharonovich, Daniel Sher
Interactions between marine microorganisms may determine the dynamics of microbial communities. Here, we show that two strains of the globally abundant marine cyanobacterium Prochlorococcus, MED4 and MIT9313, which belong to two different ecotypes, differ markedly in their response to co-culture with a marine heterotrophic bacterium, Alteromonas macleodii strain HOT1A3. HOT1A3 enhanced the growth of MIT9313 at low cell densities, yet inhibited it at a higher concentration, whereas it had no effect on MED4 growth...
April 29, 2016: ISME Journal
Christopher J Thibodeaux, Joshua Wagoner, Yi Yu, Wilfred A van der Donk
The mechanisms by which lanthipeptide synthetases control the order in which they catalyze multiple chemical processes are poorly understood. The lacticin 481 synthetase (LctM) cleaves eight chemical bonds and forms six new chemical bonds in a controlled and ordered process. Two general mechanisms have been suggested for the temporal and spatial control of these transformations. In the spatial positioning model, leader peptide binding promotes certain reactions by establishing the spatial orientation of the substrate peptide relative to the synthetase active sites...
May 25, 2016: Journal of the American Chemical Society
Xiling Zhao, Wilfred A van der Donk
The discovery of new ribosomally synthesized and post-translationally modified peptide natural products (RiPPs) has greatly benefitted from the influx of genomic information. The lanthipeptides are a subset of this class of compounds. Adopting the genome-mining approach revealed a novel lanthipeptide gene cluster encoded in the genome of Ruminococcus flavefaciens FD-1, an anaerobic bacterium that is an important member of the rumen microbiota of livestock. The post-translationally modified peptides were produced via heterologous expression in Escherichia coli...
February 18, 2016: Cell Chemical Biology
Stefano Donadio
New tools and molecules are spurring a renewed interest in natural products. In this issue of Cell Chemical Biology, Zhao and van der Donk (2016) report a single lantibiotic cluster encoding different α- and β-peptides, each with its dedicated processing enzyme. A number of clever experiments led to in vitro production of these molecules.
February 18, 2016: Cell Chemical Biology
Zheng Zhang, Li Zhang, Jie Zhang, Hongchu Ma, Shutao Sun, Jin Zhong
OBJECTIVE: To obtain the cryptic lanthipeptide from Streptomyces clavuligerus by semi-in vitro biosynthesis that is a novel method for mining lanthipeptides resource from Streptomyces. METHODS: The core peptide of cryptic lanthipeptide was modified in E. coli by nisin modification system, and purified by affinity chromatography and High Performance Liquid Chromatography (HPLC). After the leader peptide was removed, the core peptide was obtained and its dehydration and cyclic structure were analyzed by MALDI-TOF MS and tandem MS...
November 4, 2015: Wei Sheng Wu Xue Bao, Acta Microbiologica Sinica
Taro Ozaki, Yukari Kurokawa, Shohei Hayashi, Naoya Oku, Shumpei Asamizu, Yasuhiro Igarashi, Hiroyasu Onaka
Dehydroalanines in goadsporin are proposed to be formed by GodF and GodG, which show slight homology to the N-terminal glutamylation and C-terminal elimination domains, respectively, of LanB, a class I lanthipeptide dehydratase. Although similar, separated-type LanBs are conserved among thiopeptides and indispensable for their biosynthesis and biological activities, these enzymes had not yet been characterized. Here, we identified goadsporin B, which has unmodified Ser4 and Ser14, from both godF and godG disruptants...
February 2, 2016: Chembiochem: a European Journal of Chemical Biology
L Dias, T Caetano, M Pinheiro, S Mendo
Bacillus methylotrophicus strains are known for their potential as plant-growth promoters and as microbial pesticides that effectively control plant diseases caused by bacteria and fungi. Over the past few years, a wide diversity of their secondary metabolites has been extensively characterized. Among these are the RiPPs lanthipeptides, which are an important and growing group of notable compounds. The increasing interest in B. methylotrophicus species, accompanied by the development of high throughput sequencing techniques, has resulted in a substantial number of full genomes being available...
December 2015: Systematic and Applied Microbiology
Natalia A Jungmann, Eric F van Herwerden, Manuela Hügelland, Roderich D Süssmuth
Lanthipeptides are ribosomally synthesized and post-translationally modified peptides bearing the characteristic amino acids lanthionine and/or labionin. Here, we report on the discovery and characterization of the stackepeptins, produced by the Actinomycete Stackebrandtia nassauensis DSM-44728(T). The stackepeptins are the first supersized class III lanthipeptides to be discovered. Unlike other class III lanthipeptides, they consist of three lanthionine/labionin moieties instead of two. In this study, both in vivo and in vitro maturation of the peptides have been investigated...
January 15, 2016: ACS Chemical Biology
Joana Barbosa, Tânia Caetano, Sónia Mendo
The increasing number of multidrug-resistant pathogens, along with the small number of new antimicrobials under development, leads to an increased need for novel alternatives. Class I and class II lanthipeptides (also known as lantibiotics) have been considered promising alternatives to classical antibiotics. In addition to their relevant medical applications, they are used as probiotics, prophylactics, preservatives, and additives in cosmetics and personal-care products. The genus Bacillus is a prolific source of bioactive compounds including ribosomally and nonribosomally synthesized antibacterial peptides...
November 25, 2015: Journal of Natural Products
Dumitrita Iftime, Martin Jasyk, Andreas Kulik, Johannes F Imhoff, Evi Stegmann, Wolfgang Wohlleben, Roderich D Süssmuth, Tilmann Weber
Lanthipeptides are ribosomally synthesized and post-translationally modified microbial secondary metabolites. Here, we report the identification and isolation of streptocollin from Streptomyces collinus Tü 365, a new member of class IV lanthipeptides. Insertion of the constitutive ermE* promoter upstream of the lanthipeptide synthetase gene stcL resulted in peptide production. The streptocollin gene cluster was heterologously expressed in S. coelicolor M1146 and M1152 with 3.5- and 5.5-fold increased yields, respectively...
December 2015: Chembiochem: a European Journal of Chemical Biology
Dumitrita Iftime, Andreas Kulik, Thomas Härtner, Sabrina Rohrer, Timo Horst Johannes Niedermeyer, Evi Stegmann, Tilmann Weber, Wolfgang Wohlleben
Streptomycetes are prolific sources of novel biologically active secondary metabolites with pharmaceutical potential. S. collinus Tü 365 is a Streptomyces strain, isolated 1972 from Kouroussa (Guinea). It is best known as producer of the antibiotic kirromycin, an inhibitor of the protein biosynthesis interacting with elongation factor EF-Tu. Genome Mining revealed 32 gene clusters encoding the biosynthesis of diverse secondary metabolites in the genome of Streptomyces collinus Tü 365, indicating an enormous biosynthetic potential of this strain...
March 2016: Journal of Industrial Microbiology & Biotechnology
Analice C Azevedo, Cláudia B P Bento, Jeronimo C Ruiz, Marisa V Queiroz, Hilário C Mantovani
Some species of ruminal bacteria are known to produce antimicrobial peptides, but the screening procedures have mostly been based on in vitro assays using standardized methods. Recent sequencing efforts have made available the genome sequences of hundreds of ruminal microorganisms. In this work, we performed genome mining of the complete and partial genome sequences of 224 ruminal bacteria and 5 ruminal archaea to determine the distribution and diversity of bacteriocin gene clusters. A total of 46 bacteriocin gene clusters were identified in 33 strains of ruminal bacteria...
October 2015: Applied and Environmental Microbiology
Shi-Hui Dong, Weixin Tang, Tiit Lukk, Yi Yu, Satish K Nair, Wilfred A van der Donk
The enterococcal cytolysin is a virulence factor consisting of two post-translationally modified peptides that synergistically kill human immune cells. Both peptides are made by CylM, a member of the LanM lanthipeptide synthetases. CylM catalyzes seven dehydrations of Ser and Thr residues and three cyclization reactions during the biosynthesis of the cytolysin large subunit. We present here the 2.2 Å resolution structure of CylM, the first structural information on a LanM. Unexpectedly, the structure reveals that the dehydratase domain of CylM resembles the catalytic core of eukaryotic lipid kinases, despite the absence of clear sequence homology...
2015: ELife
Noah A Bindman, Silvia C Bobeica, Wenshe R Liu, Wilfred A van der Donk
The biosynthesis of ribosomally synthesized and post-translationally modified peptide (RiPP) natural products typically involves a precursor peptide which contains a leader peptide that is important for the modification process, and that is removed in the final step by a protease. Genome mining efforts for new RiPPs are often hampered by the lack of a general method to remove the leader peptides. We describe here the incorporation of hydroxy acids into the precursor peptides in E. coli which results in connection of the leader peptide via an ester linkage that is readily cleaved by simple hydrolysis...
June 10, 2015: Journal of the American Chemical Society
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