Transporters of the RND superfamily are well-known as the major drug efflux pumps of Gram-negative bacteria. However, they are widespread in organisms ranging from Archaea to Eukaryotes, and perform diverse functions. This review gives a brief overview of these diverse members of the superfamily with emphasis on their structure and functions.
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http://dx.doi.org/10.1016/j.resmic.2018.03.001 | DOI Listing |
BMC Med
January 2025
Physiological Institute, University of Regensburg, University Street 31, 93053, Regensburg, Germany.
Background: Dystonia is a common neurological hyperkinetic movement disorder that can be caused by mutations in anoctamin 3 (ANO3, TMEM16C), a phospholipid scramblase and ion channel. We previously reported patients that were heterozygous for the ANO3 variants S651N, V561L, A599D and S651N, which cause dystonia by unknown mechanisms.
Methods: We applied electrophysiology, Ca measurements and cell biological methods to analyze the molecular mechanisms that lead to aberrant intracellular Ca signals and defective activation of K channels in patients heterozygous for the ANO3 variants.
Mikrobiyol Bul
October 2024
İnönü University Faculty of Medicine, Deparment of Medical Microbiology, Malatya, Türkiye.
The increasing antibiotic resistance in Pseudomonas aeruginosa, responsible for both community-acquired and hospital-acquired infections, is of global significance. The primary mechanisms contributing to resistance development in P.aeruginosa include the increased activity of efflux pumps, decreased permeability of outer membrane porins and the production of carbapenemases.
View Article and Find Full Text PDFbioRxiv
November 2024
Institute of Biochemistry, Goethe-University Frankfurt, Germany.
Antibiotic efflux plays a key role for the multidrug resistance in Gram-negative bacteria. Multidrug efflux pumps of the resistance nodulation and cell division (RND) superfamily function as part of cell envelope spanning systems and provide resistance to diverse antibiotics. Here, we identify two phylogenetic clusters of RND proteins with conserved binding pocket residues.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
December 2024
Department of Veterinary Microbiology and Preventive Medicine, College of Veterinary Medicine, Iowa State University, Ames, IA 50011.
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