scholarly journals An ATP-binding Cassette Multidrug-Resistance Transporter Is Necessary for Tolerance of Gibberella pulicaris to Phytoalexins and Virulence on Potato Tubers

2002 ◽  
Vol 15 (2) ◽  
pp. 102-108 ◽  
Author(s):  
André Fleiβner ◽  
Claudia Sopalla ◽  
Klaus-Michael Weltring
Keyword(s):  
Abc Transporter ◽  
Magnaporthe Grisea ◽  
Atp Binding ◽  
Potato Tubers ◽  
Necrotrophic Pathogen ◽  
Defense Compounds ◽  
Gibberella Pulicaris ◽  
High Sequence Homology ◽  
Multidrug Resistance Transporter ◽  
Atp Binding Cassette

The necrotrophic pathogen Gibberella pulicaris infects potato tubers through wounds that contain fungitoxic secondary metabolites such as the phytoalexins rishitin and lubimin. In order to colonize tuber tissue, the fungus must possess a mechanism to tolerate potato defense compounds. In this paper, we show that a gene, Gpabc1, that codes an ATP-binding cassette (ABC) transporter is required for tolerance to these phytoalexins and for virulence on potato. The Gpabc1 gene, isolated in the course of a differential cDNA screen, shares high sequence homology with the ABC1 gene of Magnaporthe grisea. G. pulicaris mutants deficient in Gpabc1 were still able to metabolize rishitin but lost their tolerance to this phytoalexin as well as their virulence on potato. These results strongly suggest that the Gpabc1-encoded ABC transporter is necessary for tolerance of G. pulicaris to rishitin and that this tolerance is required for virulence on potato.

scholarly journals The human ATP-binding cassette (ABC) transporter superfamily

2001 ◽  
Vol 42 (7) ◽  
pp. 1007-1017 ◽  
Author(s):  
Michael Dean ◽  
Yannick Hamon ◽  
Giovanna Chimini
Keyword(s):  
Abc Transporter ◽  
Atp Binding ◽  
Atp Binding Cassette

scholarly journals Nucleotide-dependent Allostery within the ABC Transporter ATP-binding Cassette

2007 ◽  
Vol 282 (31) ◽  
pp. 22793-22803 ◽  
Author(s):  
Peter M. Jones ◽  
Anthony M. George
Keyword(s):  
Abc Transporter ◽  
Atp Binding ◽  
Atp Binding Cassette

scholarly journals ATP Binding Cassette Transporter A1 is Involved in Extracellular Secretion of Acetylated APE1/Ref-1

2019 ◽  
Vol 20 (13) ◽  
pp. 3178 ◽  
Author(s):  
Yu Ran Lee ◽  
Hee Kyoung Joo ◽  
Eun Ok Lee ◽  
Hyun Sil Cho ◽  
Sunga Choi ◽  
...  
Keyword(s):  
Abc Transporter ◽  
Abc Transporters ◽  
Secretory Pathway ◽  
Trichostatin A ◽  
Atp Binding ◽  
Terminal Protein ◽  
Secretion Signal ◽  
Extracellular Secretion ◽  
Atp Binding Cassette Transporter ◽  
Atp Binding Cassette

Acetylation of nuclear apurinic/apyrimidinic endonuclease-1/redox factor-1 (APE1/Ref-1) is associated with its extracellular secretion, despite the lack of an N-terminal protein secretion signal. In this study, we investigated plasma membrane targeting and translocation of APE1/Ref-1 in HEK293T cells with enhanced acetylation. While APE1/Ref-1 targeting was not affected by inhibition of the endoplasmic reticulum/Golgi-dependent secretion, its secretion was reduced by inhibitors of ATP-binding cassette (ABC) transporters, and siRNA-mediated down-regulation of ABC transporter A1. The association between APE1/Ref-1 and ABCA1 transporter was confirmed by proximal ligation assay and immunoprecipitation experiments. An APE1/Ref-1 construct with mutated acetylation sites (K6/K7R) showed reduced co-localization with ABC transporter A1. Exposure of trichostatin A (TSA) induced the acetylation of APE1/Ref-1, which translocated into membrane fraction. Taken together, acetylation of APE1/Ref-1 is considered to be necessary for its extracellular targeting via non-classical secretory pathway using the ABCA1 transporter.

scholarly journals Cystathionine β-Synthase (CBS) Domains 1 and 2 Fulfill Different Roles in Ionic Strength Sensing of the ATP-binding Cassette (ABC) Transporter OpuA

2011 ◽  
Vol 286 (43) ◽  
pp. 37280-37291 ◽  
Author(s):  
Akira Karasawa ◽  
Guus B. Erkens ◽  
Ronnie P.-A. Berntsson ◽  
Renee Otten ◽  
Gea K. Schuurman-Wolters ◽  
...  
Keyword(s):  
Ionic Strength ◽  
Abc Transporter ◽  
Atp Binding ◽  
Cbs Domains ◽  
Atp Binding Cassette

scholarly journals Mutations that alter the transmembrane signalling pathway in an ATP binding cassette (ABC) transporter.

1994 ◽  
Vol 13 (7) ◽  
pp. 1752-1759 ◽  
Author(s):  
K.M. Covitz ◽  
C.H. Panagiotidis ◽  
L.I. Hor ◽  
M. Reyes ◽  
N.A. Treptow ◽  
...  
Keyword(s):  
Abc Transporter ◽  
Signalling Pathway ◽  
Atp Binding ◽  
Transmembrane Signalling ◽  
Atp Binding Cassette

scholarly journals Role of ATP-Binding-Cassette Transporter Genes in High-Frequency Acquisition of Resistance to Azole Antifungals in Candida glabrata

2001 ◽  
Vol 45 (4) ◽  
pp. 1174-1183 ◽  
Author(s):  
Dominique Sanglard ◽  
Francoise Ischer ◽  
Jacques Bille
Keyword(s):  
Abc Transporter ◽  
High Frequency ◽  
Candida Glabrata ◽  
Antifungal Agents ◽  
Clinical Isolates ◽  
Azole Resistance ◽  
Atp Binding ◽  
Transporter Gene ◽  
Atp Binding Cassette

ABSTRACT Candida glabrata has been often isolated from AIDS patients with oropharyngeal candidiasis treated with azole antifungal agents, especially fluconazole. We recently showed that the ATP-binding-cassette (ABC) transporter gene CgCDR1 was upregulated in C. glabrata clinical isolates resistant to azole antifungal agents (D. Sanglard, F. Ischer, D. Calabrese, P. A. Majcherczyk, and J. Bille, Antimicrob. Agents Chemother. 43:2753–2765, 1999). Deletion of CgCDR1 in C. glabrata rendered the null mutant hypersusceptible to azole derivatives and showed the importance of this gene in mediating azole resistance. We observed that wild-type C. glabrata exposed to fluconazole in a medium containing the drug at 50 μg/ml developed resistance to this agent and other azoles at a surprisingly high frequency (2 × 10−4 to 4 × 10−4). We show here that this high-frequency azole resistance (HFAR) acquired in vitro was due, at least in part, to the upregulation ofCgCDR1. The CgCDR1 deletion mutant DSY1041 could still develop HFAR but in a medium containing fluconazole at 5 μg/ml. In the HFAR strain derived from DSY1041, a distinct ABC transporter gene similar to CgCDR1, calledCgCDR2, was upregulated. This gene was slightly expressed in clinical isolates but was upregulated in strains with the HFAR phenotype. Deletion of both CgCDR1 and CgCDR2suppressed the development of HFAR in a medium containing fluconazole at 5 μg/ml, showing that both genes are important mediators of resistance to azole derivatives in C. glabrata. We also show here that the HFAR phenomenon was linked to the loss of mitochondria in C. glabrata. Mitochondrial loss could be obtained by treatment with ethidium bromide and resulted in acquisition of resistance to azole derivatives without previous exposure to these agents. Azole resistance obtained in vitro by HFAR or by agents stimulating mitochondrial loss was at least linked to the upregulation of both CgCDR1 and CgCDR2.

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