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Saccharomyces cerevisiae 14‐3‐3 proteins Bmh1 and Bmh2 participate in the process of catabolite inactivation of maltose permease
Author(s) -
Mayordomo Isabel,
Regelmann Jochen,
Horak Jaroslav,
Sanz Pascual
Publication year - 2003
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(03)00498-8
Subject(s) - lactose permease , maltose , catabolite repression , yeast , saccharomyces cerevisiae , permease , biochemistry , protein subunit , phosphatase , biology , maltose binding protein , transporter , gene , sucrose , enzyme , mutant , fusion protein , recombinant dna
In this study we show that Reg1, the regulatory subunit of the Reg1/Glc7 protein phosphatase (PP1) complex, interacts physically with the two yeast members of the 14‐3‐3 protein family, Bmh1 and Bmh2. By using different fragments of the Reg1 protein we mapped the interaction domain at the N‐terminal part of the protein. We also show that Reg1 and yeast 14‐3‐3 proteins participate actively in the regulation of the glucose‐induced degradation of maltose permease (Mal61).