Cu(I)-thionein release from copper-loaded yeast cells.
The release of intact Cu(I)8-thionein from copper-resistant copper-loaded yeast cells, strain X2180-1Aa, has been shown. This copper(I)-thiolate-rich protein was characterized and compared with the chemical and physiocochemical properties of intracellular yeast Cu-thionein. The same molecular mass and stoichiometry of 8 mol copper atoms/mol protein was found. No detectable difference between the Cu-thioneins was seen in luminescence emission, electronic absorption in the ultraviolet region, chiroptical data or amino acid composition. The importance of stable Cu(I)-thiolates in Cu-thionein as a safe vehicle for transporting copper in a non-reactive manner is confirmed.
Felix
K
K
Physiologisch-Chemisches Institut, Universität Tübingen, Federal Republic of Germany.
Hartmann
H J
HJ
Weser
U
U
D002352:Carrier Proteins; D003300:Copper / Q000378:metabolism*; D008668:Metallothionein / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism*
C500769:CUP1-1 protein, S cerevisiae; D002352:Carrier Proteins; C007121:copper thionein; D003300:Copper; D008668:Metallothionein