Abstract
The plant pleiotropic drug resistance (PDR) family of ATP-binding cassette (ABC) transporters has comprehensively been researched in relation to transport of antifungal agents and resistant pathogens. In our study, analyses of the whole family of PDR genes present in the potato genome were provided. This analysis resolves discrepancies of potato PDR proteins and provides an expression analysis of all annotated potato PDR genes based on RNA-seq data. The results indicate that the potato genome contains 76 encoding PDR proteins and that these genes show a specific expression patterns, both at the organ level and in response to various hormonal treatment. These data provide some clues for future molecular genetic analysis of this important subfamily of ABC transporters. In addition, potato PDR genes may also play some important roles in the transportation of antifungal agents and resistant pathogens. Key words: ABC transporter, potato, pleiotropic drug resistance (PDR), RNA-seq.
Highlights
ATP-binding cassette (ABC) transporters have some implications in the active movement of a wide variety of substrates across cellular membranes (Higgins, 1992)
Genes; while a total of 30 pleiotropic drug resistance (PDR) protein sequences were more than 500 amino acids, which were regarded as half
The data presented in this paper provide a definitive annotation of the genomic sequences encoding this family of transporter in potato and indicate that potato contains 76 gene encoding PDR proteins
Summary
ATP-binding cassette (ABC) transporters have some implications in the active movement of a wide variety of substrates across cellular membranes (Higgins, 1992). They are involved in accumulating plants secondary metabolites in specialized organs, such as organic acids, alkaloids, lipids; transport hormones, accumulate detoxification and enhance defence in plant (Yazaki, 2006; Knöller et al, 2011). The proteins consist of one or two cytosolically oriented nubleotide-binding folds (NBFs) or ATP-binding cassettes (ABCs) linked to multiple (usually six) hydrophobic transmembrane-spanning (TMS) domains. The ABC domains are highly conserved and contain an ATP-binding site consisting of a Walker A box and Walker B box. Every box consists of approximately 120 amino acids (Walker et al, 1982); a consensus sequence specific for ABC trans-
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