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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.

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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:In this project, the proximal proteins of the balhimycin transporter Tba in A. balhimycina were investigated in order to elucidate potential interaction partners. Tba is an ABC transporter, which is co-encoded with biosynthetic enzymes in the biosynthetic gene cluster of the glycopeptide antibiotic (GPA) balhimycin. Little is known about the interactions and regulatory roles of GPA exporters. Therefore, a proximity biotinylation approach was used to label proximal proteins prior to identification by mass spectrometry. Tba was expressed as a fusion protein with the promiscuous biotin ligase TurboID.

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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.

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