Open AccessCa 2+ ‐transporting ATPase(s) of the reticulum type in intracellular membranes of Saccharomyces cerevisiae : biochemical identification
Author(s) -
Okorokov Lev A,
Kuranov Andrei Ju,
Kuranova Evgenia V,
Santos Silva Robson
Publication year - 1997
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1997.tb10168.x
Subject(s) - membrane , cyclopiazonic acid , biochemistry , endoplasmic reticulum , yeast , atpase , calmodulin , saccharomyces cerevisiae , intracellular , golgi apparatus , f atpase , biology , chemistry , enzyme , thylakoid , chloroplast , gene
Several lines of evidence are presented to show that the Ca 2+ ‐ATPase activity of total yeast membranes is due to the reticulum (R) type of Ca 2+ ‐ATPase: (1) Neither calmodulin nor low concentrations of calmodulin antagonists change Ca 2+ uptake; (2) removal of plasma membranes (PM) following Con A treatment of spheroplasts (SP) does not significantly alter Ca 2+ uptake by the remaining membranes, but increases its specific activity 3.5‐fold; (3) after incubation of membranes with [γ‐ 32 P]ATP, SDS‐PAGE shows the formation of acyl phosphate intermediates with molecular masses of around 100, 180–190 and 205 kDa; formation of these acyl phosphates requires Ca 2+ and is blocked by cyclopiazonic acid, La 3+ ions and in the absence of Ca 2+ . The data on fractionation of yeast membranes are consistent with the suggestion that both the ER and the Golgi are equipped with Ca 2+ ‐ATPase(s).