Cd2+- or Hg2+-binding proteins can replace the Cu+-chaperone Atx1 in delivering Cu+ to the secretory pathway in yeast

Copper delivery to Ccc2 – the Golgi Cu+-ATPase – was investigated in vivo, replacing the Cu+-chaperone Atx1 by various structural homologues in an atx1-Δ yeast strain. Various proteins, displaying the same ferredoxin-like fold and (M/L)(T/S)CXXC metal-binding motif as Atx1 and known as Cu+-, Cd2+- o...

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Veröffentlicht in:	FEBS letters 2005-02, Vol.579 (5), p.1117-1123
Hauptverfasser:	Morin, Isabelle, Cuillel, Martine, Lowe, Jennifer, Crouzy, Serge, Guillain, Florent, Mintz, Elisabeth
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Binding Sites Biochemistry, Molecular Biology Cadmium Cadmium - metabolism Carrier Proteins Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism Cation Transport Proteins Cation Transport Proteins - chemistry Cation Transport Proteins - genetics Cation Transport Proteins - metabolism Ccc2 Copper Copper - metabolism Cu+-homeostasis CXXC electrostatic potential surface EPS Genetic Complementation Test Heavy-metal Homeostasis Homeostasis - drug effects Life Sciences Mbd Mercury Mercury - metabolism metal-binding domain Metallo-chaperone Models, Molecular Molecular Chaperones Molecular Chaperones - chemistry Molecular Chaperones - genetics Molecular Chaperones - metabolism Molecular Sequence Data P1-type ATPase Protein Structure, Tertiary Saccharomyces cerevisiae Saccharomyces cerevisiae - drug effects Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Sequence Alignment
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