Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
NCBI PubMed ID: 33076920Publication DOI: 10.1186/s12934-020-01454-6Journal NLM ID: 101139812Publisher: London: BioMed Central
Correspondence: sunxi
tjau.edu.cn
Institutions: College of Biological Engineering, Tianjin Agricultural University, Tianjin, China, Tianjin Engineering Research Center of Agricultural Products Processing, Tianjin, China, Frontier Science Center for Synthetic Biology and Key Laboratory of Systems Bioengineering (Ministry of Education), Tianjin University, Tianjin, China, Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), School of Chemical Engineering and Technology, Tianjin University, Tianjin, China, Experiments and Teaching Center for Agricultural Analysis, Tianjin Agricultural University, Tianjin, China
In Saccharomyces cerevisiae, α-glucosidase (maltase) is a key enzyme in maltose metabolism. In addition, the overexpression of the α-glucosidase-encoding gene MAL62 has been shown to increase the freezing tolerance of yeast in lean dough. However, its cryoprotection mechanism is still not clear. RNA sequencing (RNA-seq) revealed that MAL62 overexpression increased uridine diphosphoglucose (UDPG)-dependent trehalose synthesis. The changes in transcript abundance were confirmed by quantitative reverse transcription-polymerase chain reaction (qRT-PCR) and enzyme activity assays. When the UDPG-dependent trehalose synthase activity was abolished, MAL62 overexpression failed to promote the synthesis of intracellular trehalose. Moreover, in strains lacking trehalose synthesis, the cell viability in the late phase of prefermentation freezing coupled with MAL62 overexpression was slightly reduced, which can be explained by the increase in the intracellular glycerol concentration. This result was consistent with the elevated transcription of glycerol synthesis pathway members. The increased freezing tolerance by MAL62 overexpression is mainly achieved by the increased trehalose content via the UDPG-dependent pathway, and glycerol also plays an important role. These findings shed new light on the mechanism of yeast response to freezing in lean bread dough and can help to improve industrial yeast strains.
glycerol, Saccharomyces cerevisiae, RNA-seq, α-glucosidase, freezing tolerant, lean dough, maltose, trehalose synthesis pathway
Structure type: oligomer
C
12H
22O
11Location inside paper: abstract
Trivial name: trehalose, trehalose dihydrate
Compound class: glucan, disaccharide, oligosaccharide, trehalose
Contained glycoepitopes: IEDB_142488,IEDB_144998,IEDB_146664,IEDB_742521,IEDB_983931,SB_192
Methods: biological assays, HPLC, cell growth, RNA sequencing, enzymatic assay, cell viability assay, gene expression, DNA extraction, centrifugation, anthrone-sulfuric acid assay, Stewart method
Enzymes that release or process the structure: maltase, UGPase, TPS1, TPS2, TPS3, TSL1
Biosynthesis and genetic data: biochemical and genetic data
Related record ID(s): 40554, 40832, 44030, 45048, 45464, 45745, 46310, 46334, 47146, 48287, 48338, 48342, 48645, 48654, 49503, 49534, 49535, 49550, 49900, 49916, 49946, 50149, 50340, 50354, 50595, 131827, 139902
NCBI Taxonomy refs (TaxIDs): 4932Reference(s) to other database(s): GTC:G92130SN, GlycomeDB:
245
Show glycosyltransferases
There is only one chemically distinct structure:
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