Fungal PDR transporters: Phylogeny, topology, motifs and function.

Authors :: Lamping E
Baret PV
Holmes AR
Monk BC
Goffeau A
Cannon RD
Source :: Fungal genetics and biology : FG & B [Fungal Genet Biol] 2010 Feb; Vol. 47 (2), pp. 127-42. Date of Electronic Publication: 2009 Oct 24.
Publication Year :: 2010
Abstract: The overexpression of pleiotropic drug resistance (PDR) efflux pumps of the ATP-binding cassette (ABC) transporter superfamily frequently correlates with multidrug resistance. Phylogenetic analysis of 349 full-size ( approximately 160kDa) PDR proteins (Pdrps) from 55 fungal species, including major fungal pathogens, identified nine separate protein clusters (A-G, H1a/H1b and H2). Fungal, plant and human ABCG-family Pdrps possess a nucleotide-binding domain [NBD] and a transmembrane domain [TMD] in a family-defining 'reverse' ABC transporter topology [NBD-TMD] that is duplicated [NBD-TMD](2) in full-size fungal and plant Pdrps. Although full-size Pdrps have similar halves indicating early gene duplication/fusion, they show asymmetry of their NBDs and extracellular loops (ELs). Members of cluster F are most symmetric and may be closely related to the evolutionary ancestor of Pdrps. Unique structural elements are predicted, new PDR-specific motifs identified, and the significance of these and other structural features discussed.<br /> (Copyright 2009 Elsevier Inc. All rights reserved.)