title: SUMO expression shortens the lag phase of Saccharomyces cerevisiae yeast growth caused by complex interactive effects of major mixed fermentation inhibitors found in hot-compressed water-treated lignocellulosic hydrolysate.
abstract: The complex inhibitory effects of inhibitors present in lignocellulose hydrolysate suppress the ethanol fermentation of Saccharomyces cerevisiae. Although the interactive inhibitory effects play important roles in the actual hydrolysate, few studies have investigated glycolaldehyde, the key inhibitor of hot-compressed water-treated lignocellulose hydrolysate. Given this challenge, we investigated the interactive effects of mixed fermentation inhibitors, including glycolaldehyde. First, we confirmed that glycolaldehyde was the most potent inhibitor in the hydrolysate and exerted interactive inhibitory effects in combination with major inhibitors. Next, through genome-wide analysis and megavariate data modeling, we identified SUMOylation as a novel potential mechanism to overcome the combinational inhibitory effects of fermentation inhibitors. Indeed, overall SUMOylation was increased and Pgk1, which produces an ATP molecule in glycolysis by substrate-level phosphorylation, was SUMOylated and degraded in response to glycolaldehyde. Augmenting the SUMO-dependent ubiquitin system in the ADH1-expressing strain significantly shortened the lag phase of growth, released cells from G2/M arrest, and improved energy status and glucose uptake in the inhibitor-containing medium. In summary, our study was the first to establish SUMOylation as a novel platform for regulating the lag phase caused by complex fermentation inhibitors.
authors.affiliation: Department of Biochemistry and Applied Biosciences, United Graduate School of Agricultural Sciences, Kagoshima University, 1-21-24, Korimoto, Kagoshima City, Kagoshima, 890-8580, Japan.
authors.forename: Lahiru N
authors.initials: LN
authors.lastname: Jayakody
authors.forename: Masafumi
authors.initials: M
authors.lastname: Kadowaki
authors.forename: Keisuke
authors.initials: K
authors.lastname: Tsuge
authors.forename: Kenta
authors.initials: K
authors.lastname: Horie
authors.forename: Akihiro
authors.initials: A
authors.lastname: Suzuki
authors.forename: Nobuyuki
authors.initials: N
authors.lastname: Hayashi
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Kitagaki
mesh_terms: D000079:Acetaldehyde / Q000031:analogs & derivatives / Q000378:metabolism / Q000633:toxicity; D000935:Antifungal Agents / Q000378:metabolism* / Q000633:toxicity*; D001709:Biotechnology / Q000379:methods; D002453:Cell Cycle; D004734:Energy Metabolism; D005285:Fermentation; D008031:Lignin / Q000378:metabolism* / Q000633:toxicity*; D025842:SUMO-1 Protein / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000187:drug effects* / Q000235:genetics / Q000254:growth & development*
chemical_list: D000935:Antifungal Agents; D025842:SUMO-1 Protein; C036909:lignocellulose; D008031:Lignin; D000079:Acetaldehyde; C010972:glycolaldehyde