Novel Streptopyrroles from Streptomyces rimosus with Bacterial Protein Histidine Kinase Inhibitory and Antimicrobial Activities.

Trew, Sally J.; Wrigley, Stephen K.; Pairet, L.; Sohal, Jasmeet Kaur; Shanu-Wilson, P.; Hayes, Martin A.; Martin, S. M.; M, Ram; Chicarelli-Robinson, M. I.; Kau, David A.; Byrne, C. V.; Wellington, Elizabeth M. H.; Moloney, Janet M.; Howard, Judith A. K.; Hupe, Donald; Olson, Eric R.

doi:10.7164/antibiotics.53.1

Cited by 38 publications

(24 citation statements)

References 12 publications

(3 reference statements)

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“…Using bacterial two-component system proteins in screening assays, compounds that inhibit sensor histidine kinases have been identified and their antibacterial and antifungal activities examined (115)(116)(117)(118)(119)(120). However, the antibacterial and antifungal properties of these drugs have not been directly connected to inhibition of two-component phosphorelay systems.…”

Section: Phosphorelays As Potential Targets Of Antifungal Therapiesmentioning

confidence: 99%

Fungal Histidine Kinases

Santos

Shiozaki

2001

Sci. STKE

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Eukaryotic cells predominantly use serine, threonine, and tyrosine phosphorylation in various intracellular signal transduction pathways. In contrast, prokaryotic organisms employ numerous "two-component" systems, in which signaling is achieved by transferring a phosphoryl group from phosphohistidine in the "sensor kinase" component to aspartate in the "response regulator" component. In the last several years, genetic screens and genome projects have identified sensor kinases and response regulators in lower eukaryotes and plants, revealing that eukaryotic organisms also make use of His-Asp phosphotransfer in a limited number of signaling pathways. Extensive studies in yeasts have demonstrated that a variation of the two-component system, a multistep "phosphorelay," is the prevailing mechanism among distantly related yeast species. In the budding yeast Saccharomyces cerevisiae, a His-Asp-His-Asp phosphorelay transmits osmotic stress signals to a mitogen-activated protein kinase (MAPK) cascade to induce adaptive responses. A phosphorelay in the fission yeast Schizosaccharomyces pombe, analogous to the S. cerevisiae phosphorelay, is responsible for MAPK activation in response to peroxide stress.Mammalian cells do not have any two-component or phosphorelay systems, although protein histidine kinases unrelated to the sensor kinase may be involved in cellular signaling. Because some phosphorelay proteins are essential for virulence of microbial pathogens, including the yeast fungus Candida albicans, novel antibiotics targeted to phosphorelays may be effective against eukaryotic pathogens without causing host cell damage.

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Section: Phosphorelays As Potential Targets Of Antifungal Therapiesmentioning

confidence: 99%

Fungal Histidine Kinases

Santos

Shiozaki

2001

Sci. STKE

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“…pound oxytetracycline (OTC) [3,4]. Other than oxytetracyclin a novel streptopyrroles from S. rimosus with protein histidine kinase having antimicrobial activities were found [5]. Extraction and purification of the antifungal compound from the S. rimosus MY02 were reported [6].…”

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confidence: 99%

“…IR spectrum of pure compound was made using KBr pellet technique[5] and showed the different peaks at cm-1 : 3351 (N H stretching of primary amine), 3806 (O H stretching of cyclohexane), 3780 (CO NH stretching of amide or amide carbonyl), 1627 (C = O), 1454 (C = C stretching of Ar H), 1358 (C N stretching of tertiary amine or dimethylamine), 1235 (C O of secondary alcohol), 1175 (C O of tertiary alco hol), 945 (C=C stretching of alkene/C H of alkene)Purification of active crude obtained from fermented broth of S. rimosus MTCC 10792 by first silica column chromatog raphy. 1-B.…”

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Purification and chemical characterization of antimicrobial compounds from a new soil isolate Streptomyces rimosus MTCC 10792

Singh

Rai

Tripathi

2013

Appl Biochem Microbiol

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A new isolate of Streptomyces sp. from soil of state Chhattisgarh (India) having broad spectrum antibacterial and antifungal activity was obtained. The active strain was identified as Streptomyces rimosus subsp. rimosus with accession number MTCC 10792 based on physiological, biochemical characteristics and 16S rRNA sequence homology studies. Antimicrobial compound produced by S. rimosus was tested against the drug resistance pathogens by the Bauer and Kirby method. The crude active metabolite was extracted using solvent n butanol and purified by silica column chromatography and HPLC method. The physico chemical characteristics of the one purified compound viz. color, melting point, solubility, elemental analy sis, ESIMS, IR, UV, 1HNMR, 13 CNMR and chemical reactions have been investigated. Purified antimicro bial compound produced by S. rimosus MTCC 10792 at concentration 25 µg/mL showed antitubercular activity against Mycobacterium tuberculosis H37Rv, Mycobacterium tuberculosis H37R as well as broad activity against all tested bacterial and fungal pathogens.

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“…Streptomycetes produce two thirds of all industrially manufactured antibiotics, and a large number of eukaryotic cell differentiation-inducers [12], apoptosis inhibitors [13] and inducers [14–16], protein C kinase inhibitors [17], and compounds with antitumor activity [18]. The production of these secondary metabolites (physiological differentiation) is usually temporally and genetically coordinated with the developmental program (morphological differentiation) when cultured in agar and is likely to respond to environmental, physiological and stress signals [19–22].…”

Section: Introductionmentioning

confidence: 99%

Evolutionary dynamics of rhomboid proteases in Streptomycetes

2015

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BackgroundProteolytic enzymes are ubiquitous and active in a myriad of biochemical pathways. One type, the rhomboids are intramembrane serine proteases that release their products extracellularly. These proteases are present in all forms of life and their function is not fully understood, although some evidence suggests they participate in cell signaling. Streptomycetes are prolific soil bacteria with diverse physiological and metabolic properties that respond to signals from other cells and from the environment. In the present study, we investigate the evolutionary dynamics of rhomboids in Streptomycetes, as this can shed light into the possible involvement of rhomboids in the complex lifestyles of these bacteria.ResultsAnalysis of Streptomyces genomes revealed that they harbor up to five divergent putative rhomboid genes (arbitrarily labeled families A–E), two of which are orthologous to rhomboids previously described in Mycobacteria. Characterization of each of these rhomboid families reveals that each group is distinctive, and has its own evolutionary history. Two of the Streptomyces rhomboid families are highly conserved across all analyzed genomes suggesting they are essential. At least one family has been horizontally transferred, while others have been lost in several genomes. Additionally, the transcription of the four rhomboid genes identified in Streptomyces coelicolor, the model organism of this genus, was verified by reverse transcription.ConclusionsUsing phylogenetic and genomic analysis, this study demonstrates the existence of five distinct families of rhomboid genes in Streptomycetes. Families A and D are present in all nine species analyzed indicating a potentially important role for these genes. The four rhomboids present in S. coelicolor are transcribed suggesting they could participate in cellular metabolism. Future studies are needed to provide insight into the involvement of rhomboids in Streptomyces physiology. We are currently constructing knock out (KO) mutants for each of the rhomboid genes from S. coelicolor and will compare the phenotypes of the KOs to the wild type strain.

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Novel Streptopyrroles from Streptomyces rimosus with Bacterial Protein Histidine Kinase Inhibitory and Antimicrobial Activities.

Cited by 38 publications

References 12 publications

Fungal Histidine Kinases

Fungal Histidine Kinases

Purification and chemical characterization of antimicrobial compounds from a new soil isolate Streptomyces rimosus MTCC 10792

Evolutionary dynamics of rhomboid proteases in Streptomycetes

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