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.
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.
Yasuda
T
T
Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
Shishido
K
K
D015815:Cell Adhesion Molecules / Q000494:pharmacology*; D005656:Fungal Proteins / Q000494:pharmacology*; D008970:Molecular Weight; D009842:Oligopeptides / Q000494:pharmacology*; D010446:Peptide Fragments / Q000494:pharmacology*; D011124:Polyporaceae / Q000737:chemistry*; D013211:Staphylococcus aureus / Q000187:drug effects; D015003:Yeasts / Q000187:drug effects*
D015815:Cell Adhesion Molecules; D005656:Fungal Proteins; D009842:Oligopeptides; D010446:Peptide Fragments; C047981:arginyl-glycyl-aspartic acid