<i>Streptomyces antibioticus</i> contains at least three oleandomycin‐resistance determinants, one of which shows similarity with proteins of the ABC‐transporter superfamily

Rodríguez, Amor; Olano, Carlos; Vilches, Carmen; Méndez, Cármen; Salas, José A.

doi:10.1111/j.1365-2958.1993.tb01601.x

Cited by 74 publications

(45 citation statements)

References 41 publications

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“…These two components are biochemically coupled and are thought to form an efflux pump (236,237). Several homologues of DrrAB have been described for different species of drug-producing Streptomyces, conferring resistance to oleandomycin, tetronasin, mithramycin, and kasugamycin (151,220,279,404). Despite the general assumption that proteins in the Dra family confer resistance to specific drugs, there is some suggestion that they are also able to function as MDR determinants.…”

Section: Class 3 Abc Systems That Are Probably Not Importersmentioning

confidence: 99%

Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems

Davidson

Dassa

Orelle

et al. 2008

Microbiol Mol Biol Rev

1,172

1,137

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SUMMARY ATP-binding cassette (ABC) systems are universally distributed among living organisms and function in many different aspects of bacterial physiology. ABC transporters are best known for their role in the import of essential nutrients and the export of toxic molecules, but they can also mediate the transport of many other physiological substrates. In a classical transport reaction, two highly conserved ATP-binding domains or subunits couple the binding/hydrolysis of ATP to the translocation of particular substrates across the membrane, through interactions with membrane-spanning domains of the transporter. Variations on this basic theme involve soluble ABC ATP-binding proteins that couple ATP hydrolysis to nontransport processes, such as DNA repair and gene expression regulation. Insights into the structure, function, and mechanism of action of bacterial ABC proteins are reported, based on phylogenetic comparisons as well as classic biochemical and genetic approaches. The availability of an increasing number of high-resolution structures has provided a valuable framework for interpretation of recent studies, and realistic models have been proposed to explain how these fascinating molecular machines use complex dynamic processes to fulfill their numerous biological functions. These advances are also important for elucidating the mechanism of action of eukaryotic ABC proteins, because functional defects in many of them are responsible for severe human inherited diseases.

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Section: Class 3 Abc Systems That Are Probably Not Importersmentioning

confidence: 99%

Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems

Davidson

Dassa

Orelle

et al. 2008

Microbiol Mol Biol Rev

1,172

1,137

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“…Most bacterial ABC drug transporters mediate the export of specific antibiotics (17,55,76,130,183,197,210,212). The first true bacterial ABC multidrug transporter was found in Lactococcus lactis (20).…”

Section: Atp-dependent Multidrug Transportersmentioning

confidence: 99%

Molecular Properties of Bacterial Multidrug Transporters

Putman

Veen

Konings

2000

Microbiol Mol Biol Rev

692

586

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SUMMARY One of the mechanisms that bacteria utilize to evade the toxic effects of antibiotics is the active extrusion of structurally unrelated drugs from the cell. Both intrinsic and acquired multidrug transporters play an important role in antibiotic resistance of several pathogens, including Neisseria gonorrhoeae, Mycobacterium tuberculosis, Staphylococcus aureus, Streptococcus pneumoniae, Pseudomonas aeruginosa, and Vibrio cholerae. Detailed knowledge of the molecular basis of drug recognition and transport by multidrug transport systems is required for the development of new antibiotics that are not extruded or of inhibitors which block the multidrug transporter and allow traditional antibiotics to be effective. This review gives an extensive overview of the currently known multidrug transporters in bacteria. Based on energetics and structural characteristics, the bacterial multidrug transporters can be classified into five distinct families. Functional reconstitution in liposomes of purified multidrug transport proteins from four families revealed that these proteins are capable of mediating the export of structurally unrelated drugs independent of accessory proteins or cytoplasmic components. On the basis of (i) mutations that affect the activity or the substrate specificity of multidrug transporters and (ii) the three-dimensional structure of the drug-binding domain of the regulatory protein BmrR, the substrate-binding site for cationic drugs is predicted to consist of a hydrophobic pocket with a buried negatively charged residue that interacts electrostatically with the positively charged substrate. The aromatic and hydrophobic amino acid residues which form the drug-binding pocket impose restrictions on the shape and size of the substrates. Kinetic analysis of drug transport by multidrug transporters provided evidence that these proteins may contain multiple substrate-binding sites.

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“…Several previously identified ABC transporters of Streptomyces spp. maintain self-resistance to, or accomplish the secretion of, antibiotics produced by those species (Linton et al 1994;Barrasa et al 1995;Olano et al 1995;Fernandez et al 1996;Ikeno et al 2000), and can be found outside the biosynthetic cluster encoding the antibiotic (Rodriguez et al 1993;Aguirrezabalaga et al 2000). Whether ecaA has a role in Act resistance or the secretion of actinorhodin has not been determined.…”

Section: Microarray Analysis Of Streptomyces Transcription Genes and Dementioning

confidence: 99%

Global analysis of growth phase responsive gene expression and regulation of antibiotic biosynthetic pathways inStreptomyces coelicolorusing DNA microarrays

Huang¹,

Lih²,

Pan³

et al. 2001

Genes Dev.

195

188

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The eubacterial species Streptomyces coelicolor proceeds through a complex growth cycle in which morphological differentiation/development is associated with a transition from primary to secondary metabolism and the production of antibiotics. We used DNA microarrays and mutational analysis to investigate the expression of individual genes and multigene antibiotic biosynthetic pathways during these events. We identified expression patterns in biosynthetic, regulatory, and ribosomal protein genes that were associated highly specifically with particular stages of development. A knowledge-based algorithm that correlates temporal changes in expression with chromosomal position identified groups of contiguous genes expressed at discrete stages of morphological development, inferred the boundaries of known antibiotic synthesis gene loci, and revealed novel physical clusters of coordinately regulated genes. Microarray analysis of RNA from cells mutated in genes regulating synthesis of the antibiotics actinorhodin (Act) and undecylprodigiosin (Red) identified proximate and distant sites that contain putative ABC transporter and two-component system genes expressed coordinately with genes of specific biosynthetic pathways and indicated the existence of two functionally and physically discrete regulons in the Red pathway.

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Streptomyces antibioticus contains at least three oleandomycin‐resistance determinants, one of which shows similarity with proteins of the ABC‐transporter superfamily

Cited by 74 publications

References 41 publications

Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems

Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems

Molecular Properties of Bacterial Multidrug Transporters

Global analysis of growth phase responsive gene expression and regulation of antibiotic biosynthetic pathways inStreptomyces coelicolorusing DNA microarrays

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