ArticleJournal of bacteriology1999
Transcriptional activation of ydeA, which encodes a member of the major facilitator superfamily, interferes with arabinose accumulation and induction of the Escherichia coli arabinose PBAD promoter.
Article in Journal of bacteriology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 29 citations in OpenAlex.
- Mutagenesis and functional analysis of SotB: A multidrug transporter of the major facilitator superfamily fromFrontiers in microbiology · 2022Article
- Escherichia coli AraJ boosts utilization of arabinose in metabolically engineered cyanobacterium Synechocystis sp. PCC 6803.AMB Express · 2021Article
- The Evolutionary Conservation of Escherichia coli Drug Efflux Pumps Supports Physiological Functions.Journal of bacteriology · 2020Review
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- A nucleotidyltransferase toxin inhibits growth ofScience advances · 2020Article
- Efflux systems in bacteria and their metabolic engineering applications.Applied microbiology and biotechnology · 2015Review
- 55.2, a phage T4 ORFan gene, encodes an inhibitor of Escherichia coli topoisomerase I and increases phage fitness.PloS one · 2015Article
- Single cell kinetics of phenotypic switching in the arabinose utilization system of E. coli.PloS one · 2014Article
- Identification and analysis of the putative pentose sugar efflux transporters in Escherichia coli.PloS one · 2012Article
- The maltodextrin system of Escherichia coli: metabolism and transport.Journal of bacteriology · 2005Article
- YfiK from Escherichia coli promotes export of O-acetylserine and cysteine.Journal of bacteriology · 2003Article
- Export of L-isoleucine from Corynebacterium glutamicum: a two-gene-encoded member of a new translocator family.Journal of bacteriology · 2002Article
- L-threonine export: use of peptides to identify a new translocator from Corynebacterium glutamicum.Journal of bacteriology · 2001Article
- Characterization of SotA and SotB, two Erwinia chrysanthemi proteins which modify isopropyl-beta-D-thiogalactopyranoside and lactose induction of the Escherichia coli lac promoter.Journal of bacteriology · 2000Article
- Escherichia coli gene ydeA encodes a major facilitator pump which exports L-arabinose and isopropyl-beta-D-thiogalactopyranoside.Journal of bacteriology · 1999Article
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3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Induction of genes expressed from the arabinose PBAD promoter is very rapid and maximal at low arabinose concentrations. We describe here two mutations that interfere with the expression of genes cloned under arabinose control. Both mutations map to the ydeA promoter and stimulate ydeA transcription; overexpression of YdeA from a multicopy plasmid confers the same phenotype. One mutation is a large deletion that creates a more efficient -35 region (ATCACA changed to TTCACA), whereas the other affects the initiation site (TTTT changed to TGTT). The ydeA gene is expressed at extremely low levels in exponentially growing wild-type cells and is not induced by arabinose. Disruption of ydeA has no detectable effect on cell growth. Thus, ydeA appears to be nonessential under usual laboratory growth conditions. The ydeA gene encodes a membrane protein with 12 putative transmembrane segments. YdeA belongs to the largest family of bacterial secondary active transporters, the major facilitator superfamily, which includes antibiotic resistance exporters, Lac permease, and the nonessential AraJ protein. Intracellular accumulation of arabinose is strongly decreased in mutant strains overexpressing YdeA, suggesting that YdeA facilitates arabinose export. Consistent with this interpretation, very high arabinose concentrations can compensate for the negative effect of ydeA transcriptional activation. Our studies (i) indicate that YdeA, when transcriptionally activated, contributes to the control of the arabinose regulon and (ii) demonstrate a new way to modulate the kinetics of induction of cloned genes.
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