A (TmHog1) gene encoding a mitogen-activated protein kinase (MAPK) homologous to Saccharomyces cerevisiae Hog1 (ScHog1) involved in hyper-osmotic stress signaling was isolated from Trichosporonoides megachiliensis SN-124A, an erythritol-producing yeast. Although TmHog1, like other Hog1 homologs, encoded a kinase catalytic domain containing TGY motif, it was 50-60 amino acid residues shorter than the ScHog1. A TmHog1 transgene rescued the osmotic sensitivity and glycerol production defect of S. cerevisiae hog1 Delta., a highly osmo-sensitive strain that does not produce glycerol, a compatible solute, during osmotic stress. Functional analyses of chimeric Hog1 proteins constructed from ScHog1 and TmHog1 sequences indicated that the C-terminal region of TmHog1 is more effective for glycerol biosynthesis than ScHog1 under osmotic stress. (C) 2012, The Society for Biotechnology, Japan. All rights reserved.