MS-271, a novel inhibitor of calmodulin-activated myosin light chain kinase from Streptomyces sp.—I. isolation, structural determination and biological properties of MS-271

Yano, Keiichi; Toki, Shinichiro; Nakanishi, Satoshi; Ochiai, Keiko; Ando, Katsuhiko; Yoshida, Mayumi; Matsuda, Yuzuru; Yamasaki, Motoo

doi:10.1016/0968-0896(95)00175-1

Cited by 43 publications

(40 citation statements)

References 16 publications

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“…Unusual lasso peptides have been reported to be produced by bacteria and to show a variety of activities including antibacterial activity (Wyss et al 1991;Helynck et al 1993;Yamasaki et al 1994;Detlefsen et al 1995;Yano et al 1996;Potterat et al 2004;Iwatsuki et al 2006;Kimura et al 2007;Knappe et al 2008;Vincent and Morero 2009). Among them, two gene clusters for microcin J25 and capistruin biosyntheses of respective Gram-negative bacteria, E. coli and Burkholderia sp., have been identified and characterized.…”

Section: Discussionmentioning

confidence: 98%

“…The lariatin type including lariatins (Iwatsuki et al 2006) and microcin J25 (Vincent and Morero 2009) has an internal linkage between the α-amino group of 1 Gly and the γ-carboyl group of 8 Glu. The anantin type, such as anantin (Wyss et al 1991), RES-701s (Yano et al 1996;Yamasaki et al 1994), propeptin (Kimura et al 2007), BI-32169 (Potterat et al 2004), and capistruin (Knappe et al 2008), has an internal linkage between the α-amino group of Gly1 and the γ-carboxyl group of Asp8 or Asp9. The siamycin type including siamycins (Detlefsen et al 1995) and aborycin (Helynck et al 1993) has an internal linkage between the α-amino group of Cys1 and the β-carboxyl group of Asp9 and two additional disulfide bridges between Cys1 and Cys13 and between Cys7 and Cys19.…”

Section: Introductionmentioning

confidence: 99%

“…For example, they include microcin J25, which shows antimicrobial activity against Gram-negative bacteria (Vincent and Morero 2009), RES701-1, which acts as an endothelin type B receptor antagonist (Yano et al 1996;Yamasaki et al 1994), RP71955, which inhibits HIV replication in cell culture (Frechet et al 1994), anantin, a peptide binding to the atrial natriuretic factor (ANF) (Wyss et al 1991), and MS-271, an inhibitor of calmodulin-activated myosin light chain kinase (Katahira et al 1996). They can be chemically classified into three types: lariatin, anantin, and siamycin types.…”

Section: Introductionmentioning

confidence: 99%

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Molecular cloning of the gene cluster for lariatin biosynthesis of Rhodococcus jostii K01-B0171

Inokoshi

Matsuhama

Miyake

et al. 2012

Appl Microbiol Biotechnol

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The biosynthetic gene cluster for lariatins A and B, anti-mycobacterial peptide antibiotics with a unique "lasso" structure, was cloned from Gram-positive bacterium Rhodococcus jostii K01-B0171. Random transposition mutagenesis using IS1415 derivative was carried out to identify a chromosomal locus involved in lariatin biosynthesis and six independent lariatin non-producing variants were obtained. Arbitrary PCR revealed that one insertion was located near the region involved in lariatin biosynthesis. Using the lariatin gene as a probe, a genomic library of R. jostii K01-B0171 was screened by colony hybridization, and two clones were obtained. Sequence analysis of these clones revealed that the gene cluster for lariatin biosynthesis spanning about 4.5 kb consisted of five open reading frames (larA to larE). We proposed that the linear precursor LarA is processed by LarB, LarC, and LarD, and the mature lariatin is exported by LarE.

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Section: Discussionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Molecular cloning of the gene cluster for lariatin biosynthesis of Rhodococcus jostii K01-B0171

Inokoshi

Matsuhama

Miyake

et al. 2012

Appl Microbiol Biotechnol

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“…34 Supplementary Table S1). [1][2][3][4][5][6][7][8][9][10][11][12][13][14]16,17,19,20,32,33 In general, all so far known lasso peptides originated from either proteobacterial or actinobacterial sources (Figure 4), even though genome mining approaches have revealed putative biosynthetic gene clusters in other phyla as well. 21,26−28 The biological activities hitherto identified for lasso peptides encompass a wide variety of functions ( Figure 2).…”

Section: Discovery Biological Activities and Biosynthesismentioning

confidence: 97%

Lasso Peptides: An Intriguing Class of Bacterial Natural Products

et al. 2015

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Natural products of peptidic origin often represent a rich source of medically relevant compounds. The synthesis of such polypeptides in nature is either initiated by deciphering the genetic code on the ribosome during the translation process or driven by ribosome-independent processes. In the latter case, highly modified bioactive peptides are assembled by multimodular enzymes designated as nonribosomal peptide synthetases (NRPS) that act as a protein-template to generate chemically diverse peptides. On the other hand, the ribosome-dependent strategy, although relying strictly on the 20-22 proteinogenic amino acids, generates structural diversity by extensive post-translational-modification. This strategy seems to be highly distributed in all kingdoms of life. One example for this is the lasso peptides, which are an emerging class of ribosomally assembled and post-translationally modified peptides (RiPPs) from bacteria that were first described in 1991. A wide range of interesting biological activities are known for these compounds, including antimicrobial, enzyme inhibitory, and receptor antagonistic activities. Since 2008, genome mining approaches allowed the targeted isolation and characterization of such molecules and helped to better understand this compound class and their biosynthesis. Their defining structural feature is a macrolactam ring that is threaded by the C-terminal tail and held in position by sterically demanding residues above and below the ring, resulting in a unique topology that is reminiscent of a lariat knot. The ring closure is achieved by an isopeptide bond formed between the N-terminal α-amino group of a glycine, alanine, serine, or cysteine and the carboxylic acid side chain of an aspartate or glutamate, which can be located at positions 7, 8, or 9 of the amino acid sequence. In this Account, we discuss the newest findings about these compounds, their biosynthesis, and their physicochemical properties. This includes the suggested mechanism through which the precursor peptide is enzymatically processed into a mature lasso peptide and crucial residues for enzymatic recognition. Furthermore, we highlight new insights considering the protease and thermal stability of lasso peptides and discuss why seven amino acid residue rings are likely to be the lower limit feasible for this compound class. To elucidate their fascinating three-dimensional structures, NMR spectroscopy is commonly employed. Therefore, the general methodology to elucidate these structures by NMR will be discussed and pitfalls for these approaches are highlighted. In addition, new tools provided by recent investigations to assess and prove the lasso topology without a complete structure elucidation will be summarized. These include techniques like ion mobility-mass spectrometry and a combined approach of thermal and carboxypeptidase treatment with subsequent LC-MS analysis. Nevertheless, even though much was learned about these compounds in recent years, their true native function and the exact enzymatic mechanism of their...

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“…Members of the first class contain two disulfide bonds and the first residue is a cysteine. This class contains four representatives: siamycin I (also called MS-271), 293,294 siamycin II and RP-71955, 295,296 and SSV-2083. 6 Class II lasso peptides do not contain disulfides and the first residue is a glycine.…”

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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MS-271, a novel inhibitor of calmodulin-activated myosin light chain kinase from Streptomyces sp.—I. isolation, structural determination and biological properties of MS-271

Cited by 43 publications

References 16 publications

Molecular cloning of the gene cluster for lariatin biosynthesis of Rhodococcus jostii K01-B0171

Molecular cloning of the gene cluster for lariatin biosynthesis of Rhodococcus jostii K01-B0171

Lasso Peptides: An Intriguing Class of Bacterial Natural Products

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

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