6533b861fe1ef96bd12c41c8

RESEARCH PRODUCT

C4-dicarboxylate metabolons: Interaction of C4-dicarboxylate transporters of Escherichia coli with cytosolic enzymes

Gottfried UndenChristopher Schubert

subject

chemistry.chemical_classificationCytosolEnzymechemistryBiochemistryFumaraseNitrogen assimilationmedicineTransporterMetabolonmedicine.disease_causeGeneEscherichia coli

description

AbstractMetabolons represent the structural organization of proteins for metabolic or regulatory pathways. Here the interaction of enzymes fumarase FumB and aspartase AspA with the C4-DC transporters DcuA and DcuB of Escherichia coli was tested by a bacterial two-hybrid (BACTH) assay in situ, or by co-chromatography (mSPINE). DcuB interacted strongly with FumB and AspA, and DcuA with AspA. The fumB-dcuB and the dcuA-aspA genes encoding the respective proteins are known for their colocalization on the genome and the production of co-transcripts. The data consistently suggest the formation of DcuB/FumB, DcuB/AspA and DcuA/AspA metabolons in fumarate respiration for the uptake of L-malate, or L-aspartate, conversion to fumarate and excretion of succinate after reduction. The DcuA/AspA metabolon catalyzes L-Asp uptake and fumarate excretion in concerted action also to provide ammonia for nitrogen assimilation.

yearjournalcountryeditionlanguage
2021-03-01
https://doi.org/10.1101/2021.03.01.433382