An upshift of the growth temperature from 26 to 40-degrees-C in the pr
esence of calcium leads to the aggregation of Kluyveromyces marxianus
cells and to the formation of flocs. Analysis of cell wall proteins, e
ither by sodium dodecyl sulphate-polyacrylamide gel electrophoresis of
extractable mannoproteins or by immunolocalization. revealed an accum
ulation of a protein with Mr 37 kDa (p37), upon flocculation. Immunolo
gical studies confirmed the homology of this protein with the glycolyt
ic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). When mRNA
isolated from cells growing at 40-degrees-C was translated in vitro, a
35 kDa newly labelled protein was synthesized and immunoprecipitation
assays showed that this protein is recognized by p37-antiserum, sugge
sting that the 35 kDa polypeptide might be an unglycosylated precursor
form of p37. The results indicated that the presence of this cell wal
l mannoprotein closely related to GAPDH is dependent on the growth tem
perature, suggesting its role as adhesin.