A mutant deficient in p37, a glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like protein, was obtained and characterized with respect to flocculation behaviour, resistance to temperatures above the optimum for growth, morphology, growth, calcofluor white sensitivity and GAPDH activity. In YPD media, the mutant cells were unable to flocculate and were thermosensitive. However, this thermosensitivity could be overcome by the presence of calcium. Calcofluor white was toxic to the mutant, indicating that the mutation affects cell wall structure. The contribution of p37 to total GAPDH activity was 25% when cells were using glucose as carbon source and 50% when cells were growing in 3% ethanol. These results indicate that p37 is likely to be involved in thermotolerance and flocculation, which can be related to its contribution to cell wall integrity.


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