ArticleThe Journal of biological chemistry2010
Characterization of a new multigene family encoding isomaltases in the yeast Saccharomyces cerevisiae, the IMA family.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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34 citing papers in PubMed, 70 citations in OpenAlex.
- α-Glucosidase-driven metabolism as a potential therapeutic vulnerability inFrontiers in microbiology · 2026Review
- Maltose and Maltotriose Transporters in Brewer'sInternational journal of molecular sciences · 2025Review
- Protein Biosynthesis and Carbon Catabolite Repression Are Transcriptionally Upregulated in Saccharomyces cerevisiae by Extracellular Fractions From Several Wine Yeast Species.Microbial biotechnology · 2025Article
- Evolutionary engineering and molecular characterization of an antimycin A-resistant Saccharomyces cerevisiae strain: the key role of pleiotropic drug resistance (PDR1).FEMS yeast research · 2025Article
- Key Amino Acid Residues of the Agt1 Transporter for Trehalose Transport byJournal of fungi (Basel, Switzerland) · 2024Article
- Structure-yeast α-glucosidase inhibitory activity relationship of 9-O-berberrubine carboxylates.Scientific reports · 2023Article
- Highly complete long-read genomes reveal pangenomic variation underlying yeast phenotypic diversity.Genome research · 2023Article
- Construction of a synthetic Saccharomyces cerevisiae pan-genome neo-chromosome.Nature communications · 2022Article
- Rapid selection response to ethanol in Saccharomyces eubayanus emulates the domestication process under brewing conditions.Microbial biotechnology · 2022Article
- Massive QTL analysis identifies pleiotropic genetic determinants for stress resistance, aroma formation, and ethanol, glycerol and isobutanol production in Saccharomyces cerevisiae.Biotechnology for biofuels · 2021Article
- Interaction of yeast Rad51 and Rad52 relieves Rad52-mediated inhibition of de novo telomere addition.PLoS genetics · 2020Article
- Assessing Population Diversity ofFrontiers in microbiology · 2020Article
- Characterization of a Maltase from an Early-Diverged Non-Conventional YeastInternational journal of molecular sciences · 2019Article
- Chromosome level assembly and comparative genome analysis confirm lager-brewing yeasts originated from a single hybridization.BMC genomics · 2019Article
- Lager-brewing yeasts in the era of modern genetics.FEMS yeast research · 2019Review
- Ability of Saccharomyces cerevisiae MC87-46 to assimilate isomaltose and its effects on sake taste.Scientific reports · 2019Article
- Iterative screening methodology enables isolation of strains with improved properties for a FACS-based screen and increased L-DOPA production.Scientific reports · 2019Article
- In vivo recombination of Saccharomyces eubayanus maltose-transporter genes yields a chimeric transporter that enables maltotriose fermentation.PLoS genetics · 2019Article
- Pervasive function and evidence for selection across standing genetic variation in S. cerevisiae.Nature communications · 2019Article
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3 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
It has been known for a long time that the yeast Saccharomyces cerevisiae can assimilate alpha-methylglucopyranoside and isomaltose. We here report the identification of 5 genes (YGR287c, YIL172c, YJL216c, YJL221c and YOL157c), which, similar to the SUCx, MALx, or HXTx multigene families, are located in the subtelomeric regions of different chromosomes. They share high nucleotide sequence identities between themselves (66-100%) and with the MALx2 genes (63-74%). Comparison of their amino acid sequences underlined a substitution of threonine by valine in region II, one of the four highly conserved regions of the alpha-glucosidase family. This change was previously shown to be sufficient to discriminate alpha-1,4- to alpha-1,6-glucosidase activity in YGR287c (Yamamoto, K., Nakayama, A., Yamamoto, Y., and Tabata, S. (2004) Eur. J. Biochem. 271, 3414-3420). We showed that each of these five genes encodes a protein with alpha-glucosidase activity on isomaltose, and we therefore renamed these genes IMA1 to IMA5 for IsoMAltase. Our results also illustrated that sequence polymorphisms among this family led to interesting variability of gene expression patterns and of catalytic efficiencies on different substrates, which altogether should account for the absence of functional redundancy for growth on isomaltose. Indeed, deletion studies revealed that IMA1/YGR287c encodes the major isomaltase and that growth on isomaltose required the presence of AGT1, which encodes an alpha-glucoside transporter. Expressions of IMA1 and IMA5/YJL216c were strongly induced by maltose, isomaltose, and alpha-methylglucopyranoside, in accordance with their regulation by the Malx3p-transcription system. The physiological relevance of this IMAx multigene family in S. cerevisiae is discussed.
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