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M206734200v1
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Papers In Press, published online ahead of print August 28, 2002
J. Biol. Chem, 10.1074/jbc.M206734200
Submitted on July 8, 2002
Revised on August 23, 2002
Accepted on August 28, 2002

Differential sensitivity between Fks1p and Fks2p against a novel beta -1,3-glucan synthase inhibitor, aerothricin1

Osamu Kondoh, Tsuyoshi Takasuka, Mikio Arisawa, Yuko Aoki, and Takahide Watanabe

Oncology dept., Nippon Roche Research Center, Kamakura, Kanagawa 247-8530

Corresponding Author: osamu.kondoh{at}roche.com

Fks1p and Fks2p are catalytic subunits of beta -1,3-glucan synthase, which synthesize beta -1,3-glucan, a main component of the cell wall in Saccharomyces cerevisiae. Although Fks1p and Fks2p are highly homologous, sharing 88.1% identity, it has been shown that Fks2p is more sensitive than Fks1p to one of echinocandin derivatives, which inhibits beta -1,3-glucan synthase activity. Here we show a similar differential sensitivity between Fks1p and Fks2p to a novel beta -1,3-glucan synthase inhibitor, Aerothricin1. To investigate the molecular mechanism of this differential sensitivity, we constructed a series of chimeric genes of FKSs and examined their sensitivity to Aerothricin1. As a result, it was shown that a region around the fourth extracellular domain of Fks2p, containing ten different amino acid residues from those of Fks1p, provided Fks1p Aerothricin1 sensitivity when the region was replaced with a corresponding region of Fks1p. In order to identify essential amino acid residues responsible for the sensitivity, each of the ten non-conserved amino acids of Fks1p was substituted into the corresponding amino acid of Fks2p by site-directed mutagenesis. Surprisingly, only one amino acid substitution of Fks1p (K1336I) conferred Fks1p the hypersensitivity to Aerothricin1. On the other hand, reverse substitution of the corresponding amino acid of Fks2p (I1355K) resulted in loss of hypersensitivity to Aerothricin1. These results suggest that the 1355th isoleucine of Fks2p plays a key role in Aerothricin1 sensitivity.


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