Sequence and transcriptional analysis of the Streptomyces glaucescens tcmAR tetracenomycin C resistance and repressor gene loci

Guilfoile, P G; Hutchinson, C. Richard

doi:10.1128/jb.174.11.3651-3658.1992

Cited by 84 publications

(68 citation statements)

References 48 publications

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“…The highest levels of similarity, extending over the complete sequence, existed with presumptive transmembrane proteins from antibiotic-producing Streptornyces, including LmrA from S. lincolnensis [6], TcmA from S. glaucescens [4] and Mmr from S. coelicolor [S], which confer resistance to lincomycin, tetracenomycin C and methylenomycin, respectively (Figs 4 and 5). In addition, a significant level of similarity was found with QacA, which confers resistance to a variety of antiseptic and desinfectant agents in Staphylococcus uureus [33] and for two proteins from S. coelicolor, ActII-ORF2 and ActV-ORF1, which appear to be implicated in the efflux of actinorhodin [2, …”

Section: Comparison Of Pur8 With Several Transporter Proteinsmentioning

confidence: 99%

The pur⁸ gene from the pur cluster of Streptomyces alboniger encodes a highly hydrophobic polypeptide which confers resistance to puromycin

Tercero

Lacalle²,

Jiménez

1993

European Journal of Biochemistry

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A novel puromycin‐resistancer determinant (pur8) was isolated from one end of the pur cluster that encodes the puromycin biosynthetic pathway from Streptomyces alboniger and expressed in Streptomyces lividans. The gene pur8 induced antibiotic resistance that was highly specific for puromycin. The nucleotide sequence of pur8 contains an open reading frame of 1512 bp whose deduced amino acid sequence encodes a polypeptide (Pur8) with 14 possible transmembrane spanning segments. It shows significant similarities to other known or putative transmembrane proteins, including a number which confer drug resistance in a variety of antibiotic‐producing Streptomyces, Gram‐positive and Gram‐negative bacteria, and some solute transporters of prokaryotic and eukaryotic origin. As is probably the case for most of these proteins, Pur8 may be involved in active puromycin efflux energized by a proton‐dependent electrochemical gradient. In addition, it could be implicated in secreting N‐acetylpuromycin, the last intermediate of the biosynthesis pathway, to the environment.

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Section: Comparison Of Pur8 With Several Transporter Proteinsmentioning

confidence: 99%

The pur⁸ gene from the pur cluster of Streptomyces alboniger encodes a highly hydrophobic polypeptide which confers resistance to puromycin

Tercero

Lacalle²,

Jiménez

1993

European Journal of Biochemistry

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“…PhlE also has structural similarity with integral membrane proteins associated with resistance which are encoded within clusters responsible for polyketide biosynthesis (Brautaset et al, 2000;Fernandez-Moreno et al, 1991;Guillfoile & Hutchinson, 1992;Marger & Saier, 1993;Molnar et al, 2000). It has been reported that phlE mutants produce less PHL than the parent strain (Bangera & Thomashow, 1996.…”

Section: Introductionmentioning

confidence: 99%

“…The phlE gene, located at the 39 end of the phlACBD operon in P. fluorescens strains (Bangera & Thomashow, 1996Delany, 1999) encodes a putative transmembrane permease with 12 predicted transmembrane segments (TMS) (Bangera & Thomashow, 1999 transporter mediating resistance to a range of structurally dissimilar drugs (Paulsen & Sukurray, 1993;Yoshida et al, 1990). PhlE also has structural similarity with integral membrane proteins associated with resistance which are encoded within clusters responsible for polyketide biosynthesis (Brautaset et al, 2000; Fernandez-Moreno et al, 1991;Guillfoile & Hutchinson, 1992;Marger & Saier, 1993;Molnar et al, 2000). It has been reported that phlE mutants produce less PHL than the parent strain (Bangera & Thomashow, 1996.…”

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confidence: 99%

The putative permease PhlE of Pseudomonas fluorescens F113 has a role in 2,4-diacetylphloroglucinol resistance and in general stress tolerance

et al. 2004

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2,4-Diacetylphloroglucinol (PHL) is the primary determinant of the biological control activity of Pseudomonas fluorescens F113. The operon phlACBD encodes enzymes responsible for PHL biosynthesis from intermediate metabolites. The phlE gene, which is located downstream of the phlACBD operon, encodes a putative permease suggested to be a member of the major facilitator superfamily with 12 transmembrane segments. PhlE has been suggested to function in PHL export. Here the sequencing of the phlE gene from P. fluorescens F113 and the construction of a phlE null mutant, F113-D3, is reported. It is shown that F113-D3 produced less PHL than F113. The ratio of cell-associated to free PHL was not significantly different between the strains, suggesting the existence of alternative transporters for PHL. The phlE mutant was, however, significantly more sensitive to high concentrations of added PHL, implicating PhlE in PHL resistance. Furthermore, the phlE mutant was more susceptible to osmotic, oxidative and heat-shock stresses. Osmotic stress induced rapid degradation of free PHL by the bacteria. Based on these results, we propose that the role of phlE in general stress tolerance is to export toxic intermediates of PHL degradation from the cells. INTRODUCTIONMany Pseudomonas fluorescens strains produce 2,4-diacetylphloroglucinol (PHL) (Bangera & Thomashow, 1996;Boruah & Kumar, 2002;Nowak-Thompson et al., 1994;Reddi & Borovkov, 1970; Sharifi-Tehrani et al., 1998). This phenolic molecule has broad-spectrum antifungal (Levy et al., 1992;Schoonbeek et al., 2002;Tomas-Lorente et al., 1989;Weller & Cook, 1983), antibacterial (Levy et al., 1992), antihelminthic (Bowden et al., 1965; Harrison et al., 1993) and phytotoxic (Keel et al., 1992;Reddi et al., 1969) activities. PHL is the primary determinant of biological control by P. fluorescens F113 (Shanahan et al., 1992). Synthesis of PHL is directed by the phlACBD genes, which are believed to constitute an operon (Bangera & Thomashow, 1996Delany, 1999). PhlD shows structural similarities with plant chalcone synthase, also called polyketide synthase type III, and is necessary but not sufficient for the synthesis of monoacetylphloroglucinol (MAPG) (Bangera & Thomashow, 1999). PhlA, PhlC and PhlB are necessary and sufficient for the transacetylation of MAPG to produce PHL (Bangera & Thomashow, 1999;Shanahan et al., 1992). The available data strongly suggest that PhlA, PhlC, PhlB and PhlD function in a multienzyme complex (Bangera & Thomashow, 1999;Delany, 1999). Expression of the phlACBD operon is subject to complex regulation (Aarons et al., 2000;Abbas et al., 2002;Bangera & Thomashow, 1999;Chou et al., 1993;Corbell & Loper, 1995;Delany, 1999; Delany et al., 2000;Duffy & Defago, 1999;Schnider-Keel et al., 2000). In addition, PHL is an autoregulator, positively influencing its own biosynthesis (Abbas et al., 2002;Schnider-Keel et al., 2000).Micro-organisms have developed various ways to resist the toxic effects of the secondary metabolites they produce. These mechanisms include expo...

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“…13 Meanwhile, RapH, RapG and RapY have been shown to contain a helix-turn-helix motif for DNA binding. 13 Although RapY exhibits sequence similarity to repressors of antibiotic export such as ActII from actinorhodin 58 and TcmR from tetracenomycin gene clusters, 59 the sequences of RapG are similar to those of the positive regulatory proteins SoxS and Rob from E. coli. 13 The N-terminal region of RapH contains a potential ATP-binding motif matching the canonical P-loop consensus.…”

Section: Biological Activities Of Rapamycin and Its Analogsmentioning

confidence: 99%

Biosynthesis of rapamycin and its regulation: past achievements and recent progress

et al. 2010

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Rapamycin and its analogs are clinically important macrolide compounds produced by Streptomyces hygroscopicus. They exhibit antifungal, immunosuppressive, antitumor, neuroprotective and antiaging activities. The core macrolactone ring of rapamycin is biosynthesized by hybrid type I modular polyketide synthase (PKS)/nonribosomal peptide synthetase systems primed with 4,5-dihydrocyclohex-1-ene-carboxylic acid. The linear polyketide chain is condensed with pipecolate by peptide synthetase, followed by cyclization to form the macrolide ring and modified by a series of post-PKS tailoring steps. The aim of this review was to outline past and recent advances in the biosynthesis and regulation of rapamycin, with an emphasis on the distinguished contributions of Professor Demain to the study of rapamycin. In addition, this article describes the biological activities as well as mechanism of action of rapamycin and its derivatives. Recent attempts to improve the productivity of rapamycin and generate diverse rapamycin analogs through mutasynthesis and mutagenesis are also introduced, along with some future perspectives.

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Sequence and transcriptional analysis of the Streptomyces glaucescens tcmAR tetracenomycin C resistance and repressor gene loci

Cited by 84 publications

References 48 publications

The pur⁸ gene from the pur cluster of Streptomyces alboniger encodes a highly hydrophobic polypeptide which confers resistance to puromycin

The pur⁸ gene from the pur cluster of Streptomyces alboniger encodes a highly hydrophobic polypeptide which confers resistance to puromycin

The putative permease PhlE of Pseudomonas fluorescens F113 has a role in 2,4-diacetylphloroglucinol resistance and in general stress tolerance

Biosynthesis of rapamycin and its regulation: past achievements and recent progress

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Sequence and transcriptional analysis of the Streptomyces glaucescens tcmAR tetracenomycin C resistance and repressor gene loci

Cited by 84 publications

References 48 publications

The pur8 gene from the pur cluster of Streptomyces alboniger encodes a highly hydrophobic polypeptide which confers resistance to puromycin

The pur8 gene from the pur cluster of Streptomyces alboniger encodes a highly hydrophobic polypeptide which confers resistance to puromycin

The putative permease PhlE of Pseudomonas fluorescens F113 has a role in 2,4-diacetylphloroglucinol resistance and in general stress tolerance

Biosynthesis of rapamycin and its regulation: past achievements and recent progress

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Product

Resources

About

The pur⁸ gene from the pur cluster of Streptomyces alboniger encodes a highly hydrophobic polypeptide which confers resistance to puromycin

The pur⁸ gene from the pur cluster of Streptomyces alboniger encodes a highly hydrophobic polypeptide which confers resistance to puromycin