The second cysteine‐rich domain of Mac1p is a potent transactivator that modulates DNA binding efficiency and functionality of the protein

FEBS Letters

Boutla, Alexandra¹  Alexandraki, Despina²  Voutsina, Alexandra²  Fragiadakis, George S² 

[1] Department of Biology, University of Crete, P.O. Box 1527, Heraklion 711 10, Crete, Greece;Foundation for Research and Technology-HELLAS, Institute of Molecular Biology and Biotechnology, P.O. Box 1527, Heraklion 711 10, Crete, Greece

关键词: Mac1p;    Transcriptional activation/repression;    DNA binding;    Yeast two-hybrid;    Metalloregulation;    Copper homeostasis;    DBD;    DNA binding domain;    AD;    DNA activation domain;    REPI/REPII;    repeat I/II;    CuRE;    copper-response element;    BCS;    bathocuproine disulfonate;   

DOI  :  10.1016/S0014-5793(01)02298-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown