ArticleProtein expression and purification2014
Expression, purification and reconstitution of the 4-hydroxybenzoate transporter PcaK from Acinetobacter sp. ADP1.
Article in Protein expression and purification, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 26 citations in OpenAlex.
- Multiple novel membrane proteins involve phthalate ester degradation inApplied and environmental microbiology · 2026Article
- Mitigating protocatechuic acid toxicity in Vibrio natriegens enables poly-3-hydroxybutyrate production from an aromatic carbon source.Applied microbiology and biotechnology · 2026Article
- Comparative genomics uncovers adaptive and biotechnological potential of Enterobacter xiangfangensis MDMC82 isolated from desert, and highlights putative core Enterobacteriaceae functions.Scientific reports · 2025Article
- Genetically encoded biosensor enabled mining, characterisation and engineering of aromatic acid MFS transporters.Journal of biological engineering · 2025Article
- Uptake system of lignin-derived aromatic acids in promising Sphingomonadaceae strains for lignin valorization through biological funneling.Scientific reports · 2025Article
- Characterization of Highly Ferulate-Tolerant Acinetobacter baylyi ADP1 Isolates by a Rapid Reverse Engineering Method.Applied and environmental microbiology · 2022Article
- DdvK, a Novel Major Facilitator Superfamily Transporter Essential for 5,5'-Dehydrodivanillate Uptake by Sphingobium sp. Strain SYK-6.Applied and environmental microbiology · 2018Article
- Activity of the purified plant ABC transporter NtPDR1 is stimulated by diterpenes and sesquiterpenes involved in constitutive and induced defenses.The Journal of biological chemistry · 2017Article
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5 authors at 1 institution in 1 country.
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Abstract
The aromatic acid:H(+) symporter family of integral membrane proteins play an important role in the microbial metabolism of aromatic compounds. Here, we show that the 4-hydroxybenzoate transporter from Acinetobacter sp. ADP1, PcaK, can be successfully overexpressed in Escherichia coli and purified by affinity chromatography. Affinity-purified PcaK is a stable, monodisperse homotrimer in the detergent n-dodecyl-β-d-maltopyranoside supplemented with cholesteryl hemisuccinate. The purified protein has α-helical secondary structure and can be reconstituted to a functional state in synthetic proteoliposomes. Asymmetric substrate transport was observed when proteoliposomes were energized by applying an electrochemical proton gradient (Δμ‾H(+)) or a membrane potential (ΔΨ) but not by ΔpH alone. PcaK was selective in transporting 4-hydroxybenzoate and 3,4-dihydroxybenzoate over closely related compounds, confirming previous reports on substrate specificity. However, PcaK also showed an unexpected preference for transporting 2-hydroxybenzoates. These results provide the basis for further detailed studies of the structure and function of this family of transporters.
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