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

Summary: The second cysteine-rich domain of Mac1p is a potent transactivator that
modulates DNA binding e¤ciency and functionality of the protein
Alexandra Voutsinaa
, George S. FragiadakisaYb
, Alexandra Boutlab
, Despina AlexandrakiaYbY
*
a
Foundation for Research and Technology-HELLAS, Institute of Molecular Biology and Biotechnology, P.O. Box 1527,
Heraklion 711 10, Crete, Greece
b
Department of Biology, University of Crete, P.O. Box 1527, Heraklion 711 10, Crete, Greece
Received 14 December 2000; revised 6 March 2001; accepted 7 March 2001
First published online 19 March 2001
Edited by Matti Saraste
Abstract Mac1p is a Saccharomyces cerevisiae DNA binding
transcription factor that activates genes involved in copper
uptake. A copper-induced N^C-terminal intramolecular interac-
tion and copper-independent homodimerization affect its func-
tion. Here, we present a functional analysis of Mac1p deletion

  

Source: Alexandraki, Despina - Institute of Molecular Biology and Biotechnology, Foundation of Research and Technology, Hellas

 

Collections: Biology and Medicine; Biotechnology