A cDNA clone specifying a cell wall protein was isolated from a Yarrow
ia lipolytica cDNA library. The cDNA library was constructed in the ex
pression vector lambda gt11, with the RNA isolated from actively growi
ng mycelial cells. The deduced amino acid sequence shows that the enco
ded protein contains an N-terminal hydrophobic signal peptide. We have
designated this protein YWP1 for (Y) under bar arrowia lipolytica cel
l (W) under bar all (P) under bar rotein. Northern hybridization ident
ified YWP1 transcript only when Y. lipolytica was growing in the mycel
ial form. The encoded protein seems to be covalently bound to the gluc
an cell wall since it is not released from the cell walls by sodium do
decyl sulphate extraction, but it is solubilized following partial deg
radation of beta-glucan by Zymolyase digestion. The protein is localiz
ed in the outer surface on the tip of the growing mycelial cells and i
s found partially cryptic in sub-apical locations, suggesting that it
participates directly in the mycelial wall architecture.