Abstract
The complete sequence of the pleiotropic drug resistance gene PDR5 from Saccharomyces cerevisiae is reported and analyzed. PDR5 encodes a 160-kDa protein with a predicted duplicated six membrane-span domain and a repeated putative ATP-binding domain. PDR5 shares this structural feature with the mammalian multidrug resistance pumps as well as the functional capacity of conferring resistance to various inhibitors upon amplification (Leppert, G., McDevitt, R., Falco, S. C., Van Dyk, T. K., Ficke, M. B., and Golin, J. (1990) Genetics 125, 13-20). The yeast PDR5 is thus a new member of the ABC (ATP-binding cassette) protein superfamily. Mutations in another yeast pleiotropic drug resistance gene, PDR1, encoding a putative transcription regulator (Balzi, E., Chen, W., Ulaszewski, S., Capieaux, E., and Goffeau, A. (1987) J. Biol. Chem. 262, 16871-16879), increase markedly the mRNA levels of the PDR5 and STE6 genes. The multidrug resistance mutations pdr1-3 and pdr1-6 also lead to considerable overexpression of the PDR5 plasma membrane protein.
Highlights
The complete sequence tohfe pleiotropic drugresist- and antisepticshave been clustered in a drug-resistance conance gene PDRb from Saccharomyces cerevisiae is ferring subfamily, which comprises the yeast aminotriareported and analyzed
We report that mutations of the yeast transcription regulator factor, PDR1, provide considerable overexpression of the PDR5 transcript butalso of the PDR5protein located in the plasma membrane
PDR5 Encodes a n ATP-binding cassette superfamily (ABC) Protein-The PDR5 gene had been previously cloned as a multicopy plasmid-borne DNA fragment capable of conferring multidrug resistance (Leppert et al, 1990)
Summary
PDR5 Encodes a n ABC Protein-The PDR5 gene had been previously cloned as a multicopy plasmid-borne DNA fragment capable of conferring multidrug resistance (Leppert et al, 1990). 60 bp upstream (position-234) from the estimated transcription starts, and two sequences corresponding to the binding consensus elements for the heat shock factor (Pelham, 1985). In the 3”flanking region of PDR5, a sequence matching the polyadenylation signal AATAAA (Proudfoot and Brownlee, 1976) was observed 54 bp downstream from thestop codon. The PDR5 gene encodes a polypeptide of 1511amino acids (Fig. 1) if the most upstream in-frame ATG is considered as start codon. This position is confirmed by the NH2-terminal amino acid sequence of thePDR5 protein,determined as described below. In the amino acid sequence, membrane-spanning segments are underlined, the Walker’s A and B and the ABC signature motifs are double underlined; the degenerated A motif is marked with dashes.
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
