Deciphering the Origin, Evolution, and Physiological Function of the Subtelomeric Aryl-Alcohol Dehydrogenase Gene Family in the Yeast Saccharomyces cerevisiae

Applied and Environmental Microbiology
Dong-Dong YangJean-Marie Francois

Abstract

Homology searches indicate thatSaccharomyces cerevisiaestrain BY4741 contains seven redundant genes that encode putative aryl-alcohol dehydrogenases (AAD). YeastAADgenes are located in subtelomeric regions of different chromosomes, and their functional role(s) remain enigmatic. Here, we show that two of these genes,AAD4andAAD14, encode functional enzymes that reduce aliphatic and aryl-aldehydes concomitant with the oxidation of cofactor NADPH, and that Aad4p and Aad14p exhibit different substrate preference patterns. Other yeastAADgenes are undergoing pseudogenization. The 5' sequence ofAAD15has been deleted from the genome. Repair of anAAD3missense mutation at the catalytically essential Tyr73residue did not result in a functional enzyme. However, ancestral-state reconstruction by fusing Aad6 with Aad16 and by N-terminal repair of Aad10 restores NADPH-dependent aryl-alcohol dehydrogenase activities. Phylogenetic analysis indicates thatAADgenes are narrowly distributed in wood-saprophyte fungi and in yeast that occupy lignocellulosic niches. Because yeastAADgenes exhibit activity on veratraldehyde, cinnamaldehyde, and vanillin, they could serve to detoxify aryl-aldehydes released during lignin degradation. However, none of thes...Continue Reading

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Methods Mentioned

BETA
enzymatic assay
Knockout
PCRs
PCR

Software Mentioned

YASARA Structure
VectorNTI Advanced
BLASTN
WU
BLAST
CLC Genomics Workbench

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