High impact information on mae2

• Under aerobic conditions, the recombinant strain expressing the mae1 and mae2 genes efficiently degraded 8 g/L of malate in a glycerol-ethanol medium within 7 days [1].
• No evidence for substrate-induced expression of mae2 was observed in the presence of 0.2% L-malate [2].
• However, transcription of mae2 was induced when cells were grown in high concentrations of glucose or under anaerobic conditions [2].
• Furthermore, two positive cis-acting elements in the mae2 promoter, UAS1 and UAS2, show homology with the DNA recognition sites of the cAMP-dependent transcription factors ADR1, AP-2, and ATF (activating transcription factor)/CREB (cAMP response element binding) [2].
• Furthermore, a strain of S. cerevisiae containing the mae1 and mae2 genes integrated in the genome efficiently degraded 5 g/l of L-malic acid in synthetic and Chenin Blanc grape musts [3].

Biological context of mae2

• The mae2 gene was mapped on chromosome III by chromoblotting [4].
• Sequence analysis of a 4.6-kb HindIII fragment containing the malic enzyme gene (mae2) of Schizosaccharomyces pombe, revealed the presence of an open reading frame of 1695 nucleotides, coding for a 565 amino acid polypeptide [4].
• Heterologous expression of the Sz. pombe malate permease (mae1) and malic enzyme (mae2) genes on plasmids in S. cerevisiae resulted in a recombinant strain of S. cerevisiae that efficiently degraded up to 8 g/l L-malic acid in synthetic grape must and 6.75 g/l L-malic acid in Chardonnay grape must [3].
• Both the Pka1 and Sty1 signal transduction pathways are involved in the induced expression of mae2 under fermentative conditions [5].

References