Analysis of Proteins Relating to Fruit Body Formation of Flammulina veltipes

Abstract

Fruit body formation of basidiomycetes is the most interesting and dynamic event in their life cycle. SDS-PAGE analysis of total proteins of F. veltipes showed that 58 and 30 kDa proteins appeared at late stages under both under fruiting and non-fruiting conditions. We compared total proteins of aerial hyphae in vegetative stage with those of fruit bodies by SDS-PAGE. Three proteins, with molecular masses of 34, 27, and 17 kDa, were expressed only in the fruit bodies. The 17 kDa protein was purified by CM-32 column chromatography and SDS-PAGE, and its partial amino acids sequence was analyzed. The N-terminus might be modified because no of PTH amino acid were detected. Alignment of two fragments obtained by trypsin digestion were LYDDVVPK and FADENFQLK, respectively. These amino acid sequences were 100% the same as cyclophilin of several other organisms. The 17 kDa protein may have a role as an intermediate of the cell signaling system in the process of fruit body formation or as a chaperon protein with PPIase activity expressed at low temperature. (Received July 11, 2000)