Chen TJ, Chi Z, Jiang H, Liu GL, Hu Z, Chi ZM Cell wall integrity is required for pullulan biosynthesis and glycogen accumulation in Aureobasidium melanogenum P16 Biochimica et Biophysica Acta: General Subjects1862(6) (2018)
1516-1526
The structure was elucidated in this paper NCBI PubMed ID:29550432 Publication DOI:10.1016/j.bbagen.2018.03.017 Journal NLM ID:0217513 Publisher: Elsevier Correspondence: Chi ZM <chiouc.edu.cn> Institutions: College of Marine Life Sciences, Ocean University of China, Qingdao, China, Laboratory for Marine Biology and Biotechnology, Qingdao National Laboratory for Marine Science and Technology, Qingdao, China, Department of Biology, Shantou University, Shantou, China
BACKGROUND: Pullulan and glycogen have many applications and physiological functions. However, to date, it has been unknown where and how the pullulan is synthesized in the yeast cells and if cell wall structure of the producer can affect pullulan and glycogen biosynthesis. METHODS: The genes related to cell wall integrity were cloned, characterized, deleted and complemented. The cell wall integrity, pullulan biosynthesis, glycogen accumulation and gene expression were examined. RESULTS: In this study, the GT6 and GT7 genes encoding different α(1,2) mannosyltransferases in Aureobasidium melanogenum P16 were cloned and characterized. The proteins deduced from both the GT6 and GT7 genes contained the conserved sequences YNMCHFWSNFEI and YSTCHFWSNFEI of a Ktr mannosyltransferase family. The removal of each gene and both the two genes caused the changes in colony and cell morphology and enhanced glycogen accumulation, leading to a reduced pullulan biosynthesis and the declined expression of many genes related to pullulan biosynthesis. The swollen cells of the disruptants were due to increased accumulation of glycogen, suggesting that uridine diphosphate glucose (UDP-glucose) was channeled to glycogen biosynthesis in the disruptants, rather than pullulan biosynthesis. Complementation of the GT6 and GT7 genes in the corresponding disruptants and growth of the disruptants in the presence of 0.6 M KCl made pullulan biosynthesis, glycogen accumulation, colony and cell morphology be restored. GENERAL SIGNIFICANCE: This is the first report that the two α1,2 mannosyltransferases were required for colony and cell morphology, glycogen accumulation and pullulan biosynthesis in the pullulan producing yeast.
α1, A. melanogenum, glycogen accumulation, pullulan biosynthesis, 2 mannosyltransferases
Methods: TLC, microscopy, Congo Red assay, centrifugation, ion exchange column Enzymes that release or process the structure: Pgm, Ugp, Ugt1, Pul1 Biosynthesis and genetic data: biochemical data, genetic data Comments, role: page allocation is given according to text of Accepted article
Related record ID(s): 41589, 48644, 48645, 49953, 49977, 49978, 49979, 49995, 49999, 50000, 50002, 50007, 50014, 50071, 50081, 50082, 50083, 50111, 50113 NCBI Taxonomy refs (TaxIDs):5579, 46634 Reference(s) to other database(s): GTC:G71532WE, CCSD:45938, CBank-STR:4859, GenDB:KY767023; GenDB:KY767024 Show glycosyltransferases
Chen TJ, Chi Z, Jiang H, Liu GL, Hu Z, Chi ZM Cell wall integrity is required for pullulan biosynthesis and glycogen accumulation in Aureobasidium melanogenum P16 Biochimica et Biophysica Acta: General Subjects1862(6) (2018)
1516-1526
NCBI PubMed ID:29550432 Publication DOI:10.1016/j.bbagen.2018.03.017 Journal NLM ID:0217513 Publisher: Elsevier Correspondence: Chi ZM <chiouc.edu.cn> Institutions: College of Marine Life Sciences, Ocean University of China, Qingdao, China, Laboratory for Marine Biology and Biotechnology, Qingdao National Laboratory for Marine Science and Technology, Qingdao, China, Department of Biology, Shantou University, Shantou, China
BACKGROUND: Pullulan and glycogen have many applications and physiological functions. However, to date, it has been unknown where and how the pullulan is synthesized in the yeast cells and if cell wall structure of the producer can affect pullulan and glycogen biosynthesis. METHODS: The genes related to cell wall integrity were cloned, characterized, deleted and complemented. The cell wall integrity, pullulan biosynthesis, glycogen accumulation and gene expression were examined. RESULTS: In this study, the GT6 and GT7 genes encoding different α(1,2) mannosyltransferases in Aureobasidium melanogenum P16 were cloned and characterized. The proteins deduced from both the GT6 and GT7 genes contained the conserved sequences YNMCHFWSNFEI and YSTCHFWSNFEI of a Ktr mannosyltransferase family. The removal of each gene and both the two genes caused the changes in colony and cell morphology and enhanced glycogen accumulation, leading to a reduced pullulan biosynthesis and the declined expression of many genes related to pullulan biosynthesis. The swollen cells of the disruptants were due to increased accumulation of glycogen, suggesting that uridine diphosphate glucose (UDP-glucose) was channeled to glycogen biosynthesis in the disruptants, rather than pullulan biosynthesis. Complementation of the GT6 and GT7 genes in the corresponding disruptants and growth of the disruptants in the presence of 0.6 M KCl made pullulan biosynthesis, glycogen accumulation, colony and cell morphology be restored. GENERAL SIGNIFICANCE: This is the first report that the two α1,2 mannosyltransferases were required for colony and cell morphology, glycogen accumulation and pullulan biosynthesis in the pullulan producing yeast.
α1, A. melanogenum, glycogen accumulation, pullulan biosynthesis, 2 mannosyltransferases
Methods: TLC, microscopy, Congo Red assay, centrifugation, ion exchange column Enzymes that release or process the structure: Glg1, Glg2, Gsy1, Gsy2, Glc2 Biosynthesis and genetic data: biochemical data, genetic data Comments, role: page allocation is given according to text of Accepted article
Related record ID(s): 48643, 48645 NCBI Taxonomy refs (TaxIDs):46634 Reference(s) to other database(s): GTC:G83973PX Show glycosyltransferases
There are 2 chemically distinct structures. Please, select:
Chen TJ, Chi Z, Jiang H, Liu GL, Hu Z, Chi ZM Cell wall integrity is required for pullulan biosynthesis and glycogen accumulation in Aureobasidium melanogenum P16 Biochimica et Biophysica Acta: General Subjects1862(6) (2018)
1516-1526
The structure was elucidated in this paper NCBI PubMed ID:29550432 Publication DOI:10.1016/j.bbagen.2018.03.017 Journal NLM ID:0217513 Publisher: Elsevier Correspondence: Chi ZM <chiouc.edu.cn> Institutions: College of Marine Life Sciences, Ocean University of China, Qingdao, China, Laboratory for Marine Biology and Biotechnology, Qingdao National Laboratory for Marine Science and Technology, Qingdao, China, Department of Biology, Shantou University, Shantou, China
BACKGROUND: Pullulan and glycogen have many applications and physiological functions. However, to date, it has been unknown where and how the pullulan is synthesized in the yeast cells and if cell wall structure of the producer can affect pullulan and glycogen biosynthesis. METHODS: The genes related to cell wall integrity were cloned, characterized, deleted and complemented. The cell wall integrity, pullulan biosynthesis, glycogen accumulation and gene expression were examined. RESULTS: In this study, the GT6 and GT7 genes encoding different α(1,2) mannosyltransferases in Aureobasidium melanogenum P16 were cloned and characterized. The proteins deduced from both the GT6 and GT7 genes contained the conserved sequences YNMCHFWSNFEI and YSTCHFWSNFEI of a Ktr mannosyltransferase family. The removal of each gene and both the two genes caused the changes in colony and cell morphology and enhanced glycogen accumulation, leading to a reduced pullulan biosynthesis and the declined expression of many genes related to pullulan biosynthesis. The swollen cells of the disruptants were due to increased accumulation of glycogen, suggesting that uridine diphosphate glucose (UDP-glucose) was channeled to glycogen biosynthesis in the disruptants, rather than pullulan biosynthesis. Complementation of the GT6 and GT7 genes in the corresponding disruptants and growth of the disruptants in the presence of 0.6 M KCl made pullulan biosynthesis, glycogen accumulation, colony and cell morphology be restored. GENERAL SIGNIFICANCE: This is the first report that the two α1,2 mannosyltransferases were required for colony and cell morphology, glycogen accumulation and pullulan biosynthesis in the pullulan producing yeast.
α1, A. melanogenum, glycogen accumulation, pullulan biosynthesis, 2 mannosyltransferases
Methods: TLC, microscopy, Congo Red assay, centrifugation, ion exchange column Biological activity: Removement of GT6 and GT7 genes leads to decreased amount of pullulan in cell wall Enzymes that release or process the structure: Tps1, Tps2 Biosynthesis and genetic data: biochemical data
Related record ID(s): 48643, 48644, 50340, 50354, 50364, 50595 NCBI Taxonomy refs (TaxIDs):46634 Reference(s) to other database(s): GTC:G92130SN, GlycomeDB:245 Show glycosyltransferases
Wu FF, Zhou CH, Zhou DD, Ou SY, Zhang XA, Huang HH Structure characterization of a novel polysaccharide from Hericium erinaceus fruiting bodies and its immunomodulatory activities Food and Function9(1) (2018)
294-306
The structure was elucidated in this paper NCBI PubMed ID:29168863 Publication DOI:10.1039/c7fo01389b Journal NLM ID:101549033 Publisher: Cambridge: Royal Society of Chemistry Correspondence: Huang HH <fehhuangscut.edu.cn> Institutions: School of Food Science and Engineering, South China University of Technology, Guangzhou, China, Guangdong Apollo Group Co., Ltd, Guangzhou, China, Department of Food Science and Engineering, Jinan University, Guangzhou, China, Agrobiological Gene Research Center, Guangdong Academy of Agricultural Sciences, Guangzhou, China
A novel polysaccharide fraction (HEP-S) was extracted and isolated from the fruiting bodies of Hericium erinaceus. Structural characterization revealed that HEP-S had an average molecular weight of 1.83 x 10^4 Da and consisted of rhamnose, fucose, mannose, glucose and galactose at a molar ratio of 1.47 : 0.93 : 1.36 : 8.68 : 4.08. Periodate oxidation-Smith degradation and NMR analysis showed that the main linkage types of HEP-S were composed of (1→)-α-D-Glc, (1→3,4)-α-D-Glc, (1→6)-α-D-Gal, (1→3,4)-β-D-Man, (1→3,6)-α-Rha and (1→2)-β-L-Fuc. The immunomodulatory assay indicated that HEP-S could significantly enhance the pinocytic and phagocytic capacity and promote the secretion of nitric oxide and pro-inflammatory cytokines by activating the corresponding mRNA and protein expression in RAW 264.7 cells involving a toll-like receptor 2 membrane receptor. Besides, HEP-S was also found to improve the adaptive immune function by enhancing T and B lymphocyte proliferation and increasing the interleukin-2, interleukin-4 and interferon-. secretion in spleen lymphocytes. These results suggested that HEP-S could be used as a potential immunoregulatory agent in functional foods.
Chain conformation, macrophage activation, Ganoderma atrum polysaccharide, in-vitro antioxidant, Orientalis l. franco, lepidium-meyenii, dendrobium-huoshanense, cordyceps-militaris, signaling pathways, antitumor-activity
Methods: 13C NMR, 1H NMR, periodate oxidation, Smith degradation, extraction, RT-PCR, statistical analysis, CC, dialysis, cytokine production, HPGPC, precipitation, phenol-sulfuric acid assay, HMBC, centrifugation, MTT, phagocytosis assay, HSQC, FT-IR, splenocyte proliferation assay, pinocytosis assay, ion exchange column Comments, role: a?Rhap is erroneously reported as 3,6-substituted, which is impossible; there is no certainty in article about assignment of linkages; published erroneous NMR spectra were removed by CSDB staff due to multiple errors in the NMR assignment