Ar. Iung et al., Mitochondrial function in cell wall glycoprotein synthesis in Saccharomyces cerevisiae NCYC 625 (wild type) and [rho(0)] mutants, APPL ENVIR, 65(12), 1999, pp. 5398-5402
We studied phosphopeptidomannans (PPMs) of two Saccharomyces cerevisiae NCY
C 625 strains (S, diastaticus): a wild type strain grown aerobically, anaer
obically, and in the presence of antimycin and a [rho(0)] mutant grown aero
bically and anaerobically, The aerobic wild-type cultures were highly flocc
ulent, but all others were weakly flocculent, Ligands implicated in floccul
ation of mutants or antimycin-treated cells were not aggregated as much by
concanavalin A as were those of the wild type, The [rho(0)] mutants and ant
imycin-treated cells differ from the wild type in PPM composition and inver
tase, acid phosphatase, and glucoamylase activities. PPMs extracted from di
fferent cells differ in the protein but not in the glycosidic moiety. The P
PMs were less stable in mitochondrion-deficient cells than in wild-type cel
ls grown aerobically, and this difference may be attributable to defective
mitochondrial function during cell wall synthesis. The reduced flocculation
of cells grown in the presence of antimycin, under anaerobiosis, or carryi
ng a [rho(0)] mutation may be the consequence of alterations of PPM structu
res which are the ligands of lectins, both involved in this cell-cell recog
nition phenomenon. These respiratory chain alterations also affect peripher
al, biologically active glycoproteins such as extracellular enzymes and per
ipheral PPMs.