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PY motifs of Rod1 are required for binding to Rsp5 and for drug resistance
Author(s) -
Andoh Tomoko,
Hirata Yuzoh,
Kikuchi Akira
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03104-6
Subject(s) - mutant , ubiquitin ligase , dna ligase , gsk 3 , saccharomyces cerevisiae , mutation , suppressor mutation , microbiology and biotechnology , chemistry , allosteric regulation , homologous chromosome , biochemistry , biology , genetics , kinase , ubiquitin , enzyme , gene
In Saccharomyces cerevisiae , the overexpression of ROD1 confers resistance to o ‐dinitrobenzene ( o ‐DNB), a representative of target drugs of glutathione S ‐transferase. The roles of Rod1 in drug resistance have remained to be determined. We isolated the rog3 mutation as a suppressor mutation of the temperature sensitivity of the strain, in that two of the total four glycogen synthase kinase 3 homologs were deleted. Rog3 is homologous to Rod1, and its overexpression also conferred resistance to o ‐DNB. Furthermore, these two proteins have PY‐motifs, and bound to Rsp5, a hect‐type ubiquitin ligase. The rsp5‐101 mutant showed sensitivity to o ‐DNB as did the rod1 mutant, a mutant Rod1 containing altered PY motifs was defective in ability to bind to Rsp5 and in conferring o ‐DNB resistance. These results suggest that interaction of Rod1 and Rsp5 is important for drug resistance.