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Two transketolase isogenes,  MmTKL1  and  MmTKL2,  isolated from  Moniliella megachiliensis  were investigated for their roles in stress response and erythritol biosynthesis. The encoded proteins were highly homologous in amino acid sequence and domain structure. Two stress response elements (STREs) were found upstream of  MmTKL1 , while no STRE was found upstream of  MmTKL2.  In contrast, two Ap-1 elements were present upstream of  MmTKL2 , but none were detected upstream of  MmTKL1 .  MmTKL2  partially complemented the aromatic amino acid auxotrophy of a  Saccharomyces cerevisiae tkl1  deletion mutant, suggesting that at least one of the  MmTKLs  functioned as a transketolase in vivo. In response to short-term osmotic stress (20% glucose or 1.2 M NaCl) in  Moniliella  cells,  MmTKL1  expression increased rapidly through the first 40 min before subsequently decreasing gradually, while  MmTKL2  expression showed no significant change. In contrast, short-term oxidative stress (0.15 mM menadione) induced considerable increases in  MmTKL2 , while  MmTKL1  expression remained low under the same conditions. Long-term osmotic stress (20% glucose) yielded increased expression of both genes starting at 12 h and continuing through 72 h. During either osmotic or oxidative stress, intracellular erythritol accumulation could clearly be correlated with the pattern of expression of either  MmTKL1  or  MmTKL2 . These results strongly suggested that  MmTKL1  is responsible primarily for the response to osmotic stress, while  MmTKL2  is responsible primarily for the response to oxidative stress. Thus, we postulate that the two transketolase isoforms of  M. megachiliensis  play distinct and complementary roles in coordinating erythritol production in response to distinct environmental stresses.

Complementary function of two transketolase isoforms from Moniliella megachiliensis in relation to stress response