scholarly journals An ATP-Binding Cassette Transporter, LaABCB11, Contributes to Alkaloid Transport in Lycoris aurea

2021 ◽  
Vol 22 (21) ◽  
pp. 11458
Author(s):  
Rong Wang ◽  
Yantong Liu ◽  
Sheng Xu ◽  
Jie Li ◽  
Jiayu Zhou ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Yeast Cells ◽  
Atp Binding ◽  
Physiological Effects ◽  
Biosynthesis Pathway ◽  
Cortical Cells ◽  
Atp Binding Cassette Transporter ◽  
Lycoris Aurea ◽  
Atp Binding Cassette

As a kind of Amaryllidaceae alkaloid which is accumulated in the species of Lycoris plants, lycorine has a range of physiological effects. The biosynthesis pathway of lycorine has been partly revealed, but the transport and accumulation mechanisms of lycorine have rarely been studied. In this study, an ATP-binding cassette (ABC) transporter from Lycoris aurea (L’Hér) Herb., namely LaABCB11, was cloned and functionally characterized. Heterologous expression showed that LaABCB11 transported lycorine in an outward direction, increased the tolerance of yeast cells to lycorine, and caused a lower lycorine accumulation in transformants than control or mutant in yeast. LaABCB11 is associated with the plasma membrane, and in situ hybridization indicated that LaABCB11 was mainly expressed in the phloem of leaves and bulbs, as well as in the cortical cells of roots. These findings suggest that LaABCB11 functions as a lycorine transport and it might be related to the translocation and accumulation of lycorine from the leaves and bulbs to the roots.

scholarly journals Expression of an ATP-binding cassette transporter-encoding gene (YOR1) is required for oligomycin resistance in Saccharomyces cerevisiae.

1995 ◽  
Vol 15 (12) ◽  
pp. 6875-6883 ◽  
Author(s):  
D J Katzmann ◽  
T C Hallstrom ◽  
M Voet ◽  
W Wysock ◽  
J Golin ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Fusion Gene ◽  
Sequence Similarity ◽  
Yeast Cells ◽  
Atp Binding ◽  
Zinc Cluster ◽  
Atp Binding Cassette Transporter ◽  
Transporter Family ◽  
Encoding Gene ◽  
Atp Binding Cassette

Semidominant mutations in the PDR1 or PDR3 gene lead to elevated resistance to cycloheximide and oligomycin. PDR1 and PDR3 have been demonstrated to encode zinc cluster transcription factors. Cycloheximide resistance mediated by PDR1 and PDR3 requires the presence of the PDR5 membrane transporter-encoding gene. However, PDR5 is not required for oligomycin resistance. Here, we isolated a gene that is necessary for PDR1- and PDR3-mediated oligomycin resistance. This locus, designated YOR1, causes a dramatic elevation in oligomycin resistance when present in multiple copies. A yor1 strain exhibits oligomycin hypersensitivity relative to an isogenic wild-type strain. In addition, loss of the YOR1 gene blocks the elevation in oligomycin resistance normally conferred by mutant forms of PDR1 or PDR3. The YOR1 gene product is predicted to be a member of the ATP-binding cassette transporter family of membrane proteins. Computer alignment indicates that Yor1p shows striking sequence similarity with multidrug resistance-associated protein, Saccharomyces cerevisiae Ycf1p, and the cystic fibrosis transmembrane conductance regulator. Use of a YOR1-lacZ fusion gene indicates that YOR1 expression is responsive to PDR1 and PDR3. While PDR5 expression is strictly dependent on the presence of PDR1 or PDR3, control of YOR1 expression has a significant PDR1/PDR3-independent component. Taken together, these data indicate that YOR1 provides the link between transcriptional regulation by PDR1 and PDR3 and oligomycin resistance of yeast cells.

scholarly journals Identification and Characterization of SNQ2, a New Multidrug ATP Binding Cassette Transporter of the Yeast Plasma Membrane

1995 ◽  
Vol 270 (30) ◽  
pp. 18150-18157 ◽  
Author(s):  
Anabelle Decottignies ◽  
Laurence Lambert ◽  
Patrice Catty ◽  
Herv Degand ◽  
Eric A. Epping ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Atp Binding ◽  
Yeast Plasma Membrane ◽  
Atp Binding Cassette Transporter ◽  
Identification And Characterization ◽  
Atp Binding Cassette

scholarly journals Purification and characterisation of the yeast plasma membrane ATP binding cassette transporter Pdr11p

PLoS ONE ◽  
2017 ◽  
Vol 12 (9) ◽  
pp. e0184236 ◽  
Author(s):  
Katrine Rude Laub ◽  
Magdalena Marek ◽  
Lyubomir Dimitrov Stanchev ◽  
Sara Abad Herrera ◽  
Tamara Kanashova ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Atp Binding ◽  
Yeast Plasma Membrane ◽  
Atp Binding Cassette Transporter ◽  
Atp Binding Cassette

scholarly journals Genetic Separation of FK506 Susceptibility and Drug Transport in the Yeast Pdr5 ATP-binding Cassette Multidrug Resistance Transporter

1998 ◽  
Vol 9 (2) ◽  
pp. 523-543 ◽  
Author(s):  
Ralf Egner ◽  
Friederike E. Rosenthal ◽  
Anastasia Kralli ◽  
Dominique Sanglard ◽  
Karl Kuchler
Keyword(s):  
Drug Resistance ◽  
Substrate Specificity ◽  
Drug Transport ◽  
Transmembrane Domain ◽  
Substrate Recognition ◽  
Yeast Cells ◽  
Atp Binding ◽  
In Vitro Mutagenesis ◽  
Atp Binding Cassette Transporter ◽  
Atp Binding Cassette

Overexpression of the yeast Pdr5 ATP-binding cassette transporter leads to pleiotropic drug resistance to a variety of structurally unrelated cytotoxic compounds. To identify Pdr5 residues involved in substrate recognition and/or drug transport, we used a combination of random in vitro mutagenesis and phenotypic screening to isolate novel mutant Pdr5 transporters with altered substrate specificity. A plasmid library containing randomly mutagenized PDR5 genes was transformed into appropriate drug-sensitive yeast cells followed by phenotypic selection of Pdr5 mutants. Selected mutant Pdr5 transporters were analyzed with respect to their expression levels, subcellular localization, drug resistance profiles to cycloheximide, rhodamines, antifungal azoles, steroids, and sensitivity to the inhibitor FK506. DNA sequencing of six PDR5 mutant genes identified amino acids important for substrate recognition, drug transport, and specific inhibition of the Pdr5 transporter. Mutations were found in each nucleotide-binding domain, the transmembrane domain 10, and, most surprisingly, even in predicted extracellular hydrophilic loops. At least some point mutations identified appear to influence folding of Pdr5, suggesting that the folded structure is a major substrate specificity determinant. Surprisingly, a S1360F exchange in transmembrane domain 10 not only caused limited substrate specificity, but also abolished Pdr5 susceptibility to inhibition by the immunosuppressant FK506. This is the first report of a mutation in a yeast ATP-binding cassette transporter that allows for the functional separation of substrate transport and inhibitor susceptibility.

scholarly journals Rice Stomatal Closure Requires Guard Cell Plasma Membrane ATP-Binding Cassette Transporter RCN1/OsABCG5

2016 ◽  
Vol 9 (3) ◽  
pp. 417-427 ◽  
Author(s):  
Shuichi Matsuda ◽  
Sho Takano ◽  
Moeko Sato ◽  
Kaoru Furukawa ◽  
Hidetaka Nagasawa ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Guard Cell ◽  
Stomatal Closure ◽  
Atp Binding ◽  
Cell Plasma Membrane ◽  
Atp Binding Cassette Transporter ◽  
Cell Plasma ◽  
Atp Binding Cassette

scholarly journals A functional study on polymorphism of the ATP-binding cassette transporter ABCG2: critical role of arginine-482 in methotrexate transport

2003 ◽  
Vol 373 (3) ◽  
pp. 767-774 ◽  
Author(s):  
Hideyuki MITOMO ◽  
Ryo KATO ◽  
Akiko ITO ◽  
Shiho KASAMATSU ◽  
Yoji IKEGAMI ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Amino Acid ◽  
Substrate Specificity ◽  
Atp Binding ◽  
Transport Activity ◽  
Hek 293 ◽  
Hek 293 Cells ◽  
Atp Binding Cassette Transporter ◽  
293 Cells ◽  
Atp Binding Cassette

Overexpression of the ATP-binding cassette transporter ABCG2 reportedly causes multidrug resistance, whereas altered drug-resistance profiles and substrate specificity are implicated for certain variant forms of ABCG2. At least three variant forms of ABCG2 have been hitherto documented on the basis of their amino acid moieties (i.e., arginine, glycine and threonine) at position 482. In the present study we have generated those ABCG2 variants by site-directed mutagenesis and expressed them in HEK-293 cells. Exogenous expression of the Arg482, Gly482, and Thr482 variant forms of ABCG2 conferred HEK-293 cell resistance toward mitoxantrone 15-, 47- and 54-fold, respectively, as compared with mock-transfected HEK-293 cells. The transport activity of those variants was examined by using plasma-membrane vesicles prepared from ABCG2-overexpressing HEK-293 cells. [Arg482]ABCG2 transports [3H]methotrexate in an ATP-dependent manner; however, no transport activity was observed with the other variants (Gly482 and Thr482). Transport of methotrexate by [Arg482]ABCG2 was significantly inhibited by mitoxantrone, doxorubicin and rhodamine 123, but not by S-octylglutathione. Furthermore, ABCG2 was found to exist in the plasma membrane as a homodimer bound via cysteinyl disulphide bond(s). Treatment with mercaptoethanol decreased its apparent molecular mass from 140 to 70 kDa. Nevertheless, ATP-dependent transport of methotrexate by [Arg482]ABCG2 was little affected by such mercaptoethanol treatment. It is concluded that Arg482 is a critical amino acid moiety in the substrate specificity and transport of ABCG2 for certain drugs, such as methotrexate.

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