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The second cysteine‐rich domain of Mac1p is a potent transactivator that modulates DNA binding efficiency and functionality of the protein
Author(s) -
Voutsina Alexandra,
Fragiadakis George S,
Boutla Alexandra,
Alexandraki Despina
Publication year - 2001
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(01)02298-0
Subject(s) - transactivation , cysteine , transcription factor , dna binding domain , dna , saccharomyces cerevisiae , dna binding protein , chemistry , binding domain , context (archaeology) , gene , transcription (linguistics) , biochemistry , microbiology and biotechnology , copper , biophysics , binding site , biology , paleontology , linguistics , philosophy , enzyme , organic chemistry
Mac1p is a Saccharomyces cerevisiae DNA binding transcription factor that activates genes involved in copper uptake. A copper‐induced N–C‐terminal intramolecular interaction and copper‐independent homodimerization affect its function. Here, we present a functional analysis of Mac1p deletion derivatives that attributes new roles to the second cysteine‐rich (REPII) domain of the protein. This domain exhibits the copper‐responsive potent transactivation function when assayed independently and, in the context of the entire protein, modulates the efficiency of Mac1p binding to DNA. The efficiency of binding to both copper‐response promoter elements can determine the in vivo functionality of Mac1p independent of homodimerization.