ArticleThe Journal of biological chemistry2013
Dual role of the metalloprotease FtsH in biogenesis of the DrrAB drug transporter.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 36 citations in OpenAlex.
- Nanoparticle-Based Approaches for Glioblastoma Treatment: Advances and Future Prospects.CNS & neurological disorders drug targets · 2026Review
- Brain Delivery Strategies for Biomacromolecular Drugs: Intranasal Administration.International journal of nanomedicine · 2025Review
- The Daunomycin: Biosynthesis, Actions, and the Search for New Solutions to Enhance Production.Microorganisms · 2024Review
- Recent Advances in Understanding the Structural and Functional Evolution of FtsH Proteases.Frontiers in plant science · 2022Review
- Bacterial bug-out bags: outer membrane vesicles and their proteins and functions.Journal of microbiology (Seoul, Korea) · 2020Review
- Nanomaterial-based blood-brain-barrier (BBB) crossing strategies.Biomaterials · 2019Review
- Depletion of the FtsH1/3 Proteolytic Complex Suppresses the Nutrient Stress Response in the CyanobacteriumThe Plant cell · 2019Article
- Biochemical characterization of the mouse ABCF3 protein, a partner of the flavivirus-resistance protein OAS1B.The Journal of biological chemistry · 2019Article
- Rewiring of the FtsH regulatory network by a single nucleotide change in saeS of Staphylococcus aureus.Scientific reports · 2017Article
- Thylakoid-Bound FtsH Proteins Facilitate Proper Biosynthesis of Photosystem I.Plant physiology · 2016Article
- Characterization of acetic acid-detoxifying Escherichia coli evolved under phosphate starvation conditions.Microbial cell factories · 2016Article
- Review
- The DrrAB efflux system of Streptomyces peucetius is a multidrug transporter of broad substrate specificity.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
This study provides the first direct evidence for the dual role of the metalloprotease FtsH in membrane protein biogenesis. Using the physiological substrate DrrAB, it is shown that FtsH is not only responsible for proteolysis of unassembled DrrB protein but also plays a much broader role in biogenesis of the DrrAB complex. Previous studies showed that the stable expression of DrrB in the membrane depends on simultaneous expression of DrrA. Here we show that DrrB is proteolyzed by FtsH when it is expressed alone. Moreover, DrrA and DrrB proteins expressed together in a temperature-sensitive ftsH mutant strain of Escherichia coli were found to be nonfunctional due to their incorrect assembly. Simultaneous expression of wild-type FtsH in trans resulted in normal doxorubicin efflux. Strikingly, doxorubicin efflux could be restored in mutant cells irrespective of whether FtsH was expressed simultaneously with DrrAB or expressed after these proteins had already accumulated in an inactive conformation, thus providing crucial evidence for the ability of FtsH to refold the misassembled proteins. Complementation experiments also showed that the catalytic AAA domain of FtsH contains a chaperone-like activity, however, unlike wild-type FtsH, it was unable to restore function. Our results therefore show for the first time that FtsH contains the protease as well as refolding functions, and both the AAA and the proteolytic domains of FtsH are required for each of these activities.
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Registered trials
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