Aggregation of yeast cells induced by the Arg-Gly-Asp motif-containing fragment of high-molecular-mass cell-adhesion protein MFBA, derived from the basidiomycetous mushroom Lentinus edodes.

Abstract

A fruiting body-specific cDNA mfbAc, derived from the basidiomycete Lentinus edodes, has been shown to encode a high-molecular-mass (2157 amino acids) cell-adhesion protein MFBA containing the Arg-Gly-Asp (RGD) motif. A 425-amino-acid fragment containing the RGD motif of MFBA (designated MFBA(582-1006) peptide) produced in Escherichia coli exhibited cell-adhesion and spreading activity toward mammalian cells and cell-aggregation activity toward basidiomycetous hyphal cells via the RGD sequence. Here we investigated the biological activity of MFBA(582-1006) peptide in Saccharomyces cerevisiae. The DNA sequence encoding MFBA(582-1006) peptide, introduced into the yeast using an expression vector, resulted in a marked aggregation of the yeast cells. The aggregation was almost completely abolished by replacement of the RGD motif by an RGE motif in the peptide sequence.