Flocculation of Saccharomyces cerevisiae is induced by transformation with the GAP1 gene from Kluyveromyces marxianus

• Type: Article in International Scientific Journal
• Date: 2000

Authors

Falcao Moreira, R (Author) Other; Ferreira Da Silva, F (Author) Other; Moradas Ferreira, P (Author) ICBAS

Journal

Title: Yeast

Vol. 16

Pages: 231-240

ISSN: 0749-503X

Publisher: Wiley-Blackwell

Indexing

ISI Web of Knowledge - 10 Citations

Scopus - 12 Citations

Scientific classification

FOS: Natural sciences > Biological sciences

Other information

Authenticus ID: P-001-105

DOI: 10.1002/(sici)1097-0061(200002)16:3<231::aid-yea530>3.0.co;2-c

Abstract (EN): A non-flocculent strain of Saccharomyces cerevisiae was transformed with the GAP1 gene which encodes p37, a GAPDH-like protein present in the cell wall of Kluyveromyces marxianus flocculent cells. The transformed cells were characterized with respect to flocculation behaviour, morphology, growth, cell wall integrity and GAPDH activity. A flocculent phenotype was acquired by the transformed cells, showing a behaviour in respect to flocculation/deflocculation very similar to that of K. marxianus. The presence of p37 in the cell wall was assessed by immunoprecipitation of biotinylated cell wall proteins and an accumulation of p37 was evident in the cell wall of transformed cells. This result was confirmed by studies using a chimeric protein resulting from fusing the p37 with a yeast-enhanced green fluorescent protein, yEGFP. The recombinant protein was localized mainly in the cell wall of the transformed strain, although the presence of p37 in the cytosol was indicated by an increase in GAPDH activity. Calcofluor white sensitivity tests indicated that the cell wall structure is affected by the accumulation of p37. These results provided further evidence of p37 function regarding flocculation and that although lacking a N-terminal signal peptide p37 is targeted to the cell wall. Copyright (C) 2000 John Wiley & Sons, Ltd.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 10