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Elucidation of the substrate specificity of the ABC transporter Tba uncovers an unsuspected role in the biosynthesis of glycopeptide antibiotics

ABSTRACT: Elucidation of the substrate specificity of the ABC transporter Tba uncovers an unsuspected role in the biosynthesis of glycopeptide antibiotics

PROVIDER: PRJNA1144888 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR30155908.fastq.gz	Fastqsanger.gz
	SRR30155909.fastq.gz	Fastqsanger.gz
	SRR30155910.fastq.gz	Fastqsanger.gz
	SRR30155911.fastq.gz	Fastqsanger.gz
	SRR30155912.fastq.gz	Fastqsanger.gz

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Elucidation of the substrate specificity of the ABC transporter Tba uncovers an unsuspected role in the biosynthesis of glycopeptide antibiotics

Project description:Glycopeptide antibiotics (GPA) such as vancomycin and teicoplanin are essential last-resort antibiotics produced by actinomycetes. Their biosynthesis is encoded within biosynthetic gene clusters, also harboring genes for regulation, and transport. Diverse types of GPAs have been characterized that differ in peptide backbone composition and modification patterns. However, little is known about the ATP-binding cassette (ABC) transporters facilitating GPA export. Employing cutting-edge techniques, we investigated the substrate specificity of GPA ABC-transporters towards the type-I GPA, balhimycin. Phylogenetic analysis and trans-complementation experiments revealed that balhimycin can only be exported by the related type I GPA transporters Tba and Tva (transporter of vancomycin). Molecular dynamics simulations and mutagenesis experiments showed that Tba exhibits specificity towards the peptide backbone rather than the attached modifications. Unexpectedly, deletion or functional inactivation of Tba halted balhimycin biosynthesis. Combined with proximity dependent biotinylation experiments this suggested that the interaction of the active transporter with the biosynthetic machinery is required for compound production.

2025-04-09 | GSE274067 | GEO

Adaptation of Cupriavidus metallidurans CH34 to toxic zinc concentrations involves an uncharacterized ABC-type transporter

Project description:Cupriavidus metallidurans CH34 is a well-studied metal-resistant β-proteobacterium and contains a battery of genes involved in the resistance and processing of numerous metals. Here, we performed a directed evolution experiment to obtain derivatives adapted to grow in the presence of zinc at concentrations above the minimal inhibitory concentration for the parental strain. Genetic characterization of one derivative, CH34ZnR, which was also more resistant to cadmium, revealed seven mutations, including inactivation of glpR coding for a DeoR-type transcriptional repressor by insertion of IS1088. The latter resulted in the constitutive expression of the neighboring ABC-type transporter. GlpR and the adjacent ABC transporter are highly similar to the glycerol operon regulator and ATP-driven glycerol importer of Rhizobium leguminosarum bv. viciae VF39, respectively. Deletion of glpR or the ABC transporter and complementation of CH34ZnR with the parental glpR gene further demonstrated that loss of GlpR function, with concomitant induction of the adjacent ABC transporter, is pivotal in the observed phenotype. Moreover, addition of glycerol, presumably by glycerol-mediated reduced GlpR activity, also promoted increased zinc and cadmium resistance. Thus, the ABC-type transporter is proposed to be a new adaptation route during exposure to toxic zinc concentrations.

2021-03-03 | GSE156826 | GEO

Transcriptional profiling of orf19.5100/MLT1 ABC transporter knockout in Candida albicans

2016-07-25 | GSE70341 | GEO

Transcriptional profiling of putative ABC Transporter gene orf19.4531 knockout in Candida albicans

Project description:Since, ABC transporters do perform various physiological roles.To get better insight about possible involvement of putative ABC transporter orf19.4531 in different functions transcriptional profiling have been peformed and compared between WT(SC5314) Candida albicans cells vs putative orf19.4531 knockout cells after 6hrs growth of culture.The assay as peformed in biological duplicate sample.

2017-12-31 | GSE70340 | GEO

Transcriptional profiling of orf19.5100/MLT1 ABC transporter knockout in Candida albicans

Project description:Recent reports have been suggested involvement of ABC transporters in various physiological roles.To get better insight about possible involvement of vacuolar ABC transporter MLT1/orf19.5100 in different physiological roles transcriptional profiling have been peformed and compared between WT(SC5314) Candida albicans cells vs putative orf19.5100 knockout cells after 6hrs growth of culture.The assay as peformed in biological duplicate sample. Agilent one-color experiment,Organism: Candida albicans ,Custom Agilent Candida albicans 8x15k Microarray Gene expression (AMADID: 026377) designed by Genotypic Technology Private Limited , Labeling kit: Agilent Quick-Amp labeling Kit (p/n5190-0442)

2016-07-25 | E-GEOD-70341 | biostudies-arrayexpress

Transcriptional profiling of putative half ABC transporter gene orf19.3120 knockout cells in Candida albicans

Project description:Inventory of ABC transporters of Candida albicans shows presence of large no of ABC transporters in its genome.The large no of such protein presence suggested that these proteins may involve in various functions.To know involvement of PM ABC transporter orf19.3120 in different physiological roles transcriptional profiling have been peformed and compared between WT(SC5314) Candida albicans cells vs orf19.3120 knockout cells after 6hrs growth of culture.The assay as peformed in biological duplicate sample.

2021-12-31 | GSE70339 | GEO

The Plasmodium falciparum protein PfMRP1 functions as an influx ABC transporter

Project description:Adenosine triphosphate (ATP)-binding cassette (ABC) transporters play an important role in mediating solute or drug transport across cellular membranes. Although this class of transporters has been well characterized in diverse organisms little is known about the physiological roles in Plasmodium falciparum, the deadliest malaria parasite species. We studied the Plasmodium falciparum Multidrug Resistance-associated Protein 1 (PfMRP1; PF3D7_0112200), an ABC transporter localized to the parasite plasma membrane, generating genetic disrupted parasites. We demonstrate that parasites with disrupted pfmrp1 are resistant to folate analogs, methotrexate and aminopterin, with antimalarial activity. This phenotype occurs due to reduction in compound accumulation in the parasite cytoplasm. Phylogenetic analysis supports pfmrp1 being distantly related to ABC transporters in other eukaryotes, suggesting an unusual function. We propose that PfMRP1 can act as a solute importer, a function not previously observed in this organism.

2022-01-31 | GSE195649 | GEO

The Plasmodium falciparum protein PfMRP1 functions as an influx ABC transporter

Project description:The Plasmodium falciparum protein PfMRP1 functions as an influx ABC transporter

| PRJNA801625 | ENA

Mass spectrometry analysis of ABC transporter proteins in pilocarpine mouse model of epilepsy

Project description:Hippocampal tissue from pilocarpine treated mice was examined by mass spectrometry to determine the change in levels of ABC transporter proteins.

2022-12-03 | PXD037454 | Pride

Structural basis for substrate specificity of an amino acid ABC transporter.

Project description:ATP-binding cassette (ABC) transporters are ubiquitous integral membrane proteins that translocate a variety of substrates, ranging from ions to macromolecules, either out of or into the cytosol (hence defined as importers or exporters, respectively). It has been demonstrated that ABC exporters and importers function through a common mechanism involving conformational switches between inward-facing and outward-facing states; however, the mechanism underlying their functions, particularly substrate recognition, remains elusive. Here we report the structures of an amino acid ABC importer Art(QN)2 from Thermoanaerobacter tengcongensis composed of homodimers each of the transmembrane domain ArtQ and the nucleotide-binding domain ArtN, either in its apo form or in complex with substrates (Arg, His) and/or ATPs. The structures reveal that the straddling of the TMDs around the twofold axis forms a substrate translocation pathway across the membrane. Interestingly, each TMD has a negatively charged pocket that together create a negatively charged internal tunnel allowing amino acids carrying positively charged groups to pass through. Our structural and functional studies provide a better understanding of how ABC transporters select and translocate their substrates.

| S-EPMC4413293 | biostudies-literature

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