Lack of endoplasmic reticulum 1,2-α-mannosidase activity that trims N-glycan Man9GlcNAc2 to Man8GlcNAc2 isomer B in a manE gene disruptant of Aspergillus oryzae

Akao, Takeshi; Yahara, Akinori; Sakamoto, Kazutoshi; Akita, Osamu; Yoshida, Takashi

doi:10.1016/j.jbiosc.2011.11.015

Cited by 7 publications

(5 citation statements)

References 11 publications

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“…The orthologues of yeast GlS2 , GTB1 , and MNS1 have been functionally characterized in A. oryzae. 48 , 49 Thus, the genes (AA1_SCon_023_0105, AA1_SCon_007_0165, and AA1_SCon_010_0597) responsible for the trimming of N -glycans in the ER are well conserved in A. luchuensis . Glycoproteins that enter the Golgi apparatus are subjected to further elongation with N -glycans.…”

Section: Resultsmentioning

confidence: 99%

Genome sequence ofAspergillus luchuensisNBRC 4314

Yamada

Machida

Hosoyama

et al. 2016

DNA Res

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Awamori is a traditional distilled beverage made from steamed Thai-Indica rice in Okinawa, Japan. For brewing the liquor, two microbes, local kuro (black) koji mold Aspergillus luchuensis and awamori yeast Saccharomyces cerevisiae are involved. In contrast, that yeasts are used for ethanol fermentation throughout the world, a characteristic of Japanese fermentation industries is the use of Aspergillus molds as a source of enzymes for the maceration and saccharification of raw materials. Here we report the draft genome of a kuro (black) koji mold, A. luchuensis NBRC 4314 (RIB 2604). The total length of nonredundant sequences was nearly 34.7 Mb, comprising approximately 2,300 contigs with 16 telomere-like sequences. In total, 11,691 genes were predicted to encode proteins. Most of the housekeeping genes, such as transcription factors and N-and O-glycosylation system, were conserved with respect to Aspergillus niger and Aspergillus oryzae. An alternative oxidase and acid-stable α-amylase regarding citric acid production and fermentation at a low pH as well as a unique glutamic peptidase were also found in the genome. Furthermore, key biosynthetic gene clusters of ochratoxin A and fumonisin B were absent when compared with A. niger genome, showing the safety of A. luchuensis for food and beverage production. This genome information will facilitate not only comparative genomics with industrial kuro-koji molds, but also molecular breeding of the molds in improvements of awamori fermentation.

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Section: Resultsmentioning

confidence: 99%

Genome sequence ofAspergillus luchuensisNBRC 4314

Yamada

Machida

Hosoyama

et al. 2016

DNA Res

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“…It removes a single mannose residue from Man 9 GlcNAc 2 , generating Man 8 GlcNAc 2 isomer B. Disruption of manE caused drastic decreases in ER-Man activity in A. oryzae microsomes. 95) II.iii. Acid activation of proyrosinase from A. oryzae Kojic acid (5-hydroxy-2-(hydroxymethyl)-4H-pyran-4-one) ( Table 2) is antibiotic substance produced by A. oryzae.…”

Section: III Aspergillopepsin I Aorsin and Serine Carboxypeptidasementioning

confidence: 96%

Development of enzyme technology for Aspergillus oryzae, A. sojae, and A. luchuensis,the national microorganisms of Japan

Ichishima

2016

Bioscience, Biotechnology, and Biochemistry

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This paper describes the modern enzymology in Japanese bioindustries. The invention of Takadiastase by Jokiti Takamine in 1894 has revolutionized the world of industrial enzyme production by fermentation. In 1949, a new γ-amylase (glucan 1,4-α-glucosidase, EC 3.2.1.3) from A. luchuensis (formerly designated as A. awamori), was found by Kitahara. RNase T1 (guanyloribonuclease, EC 3.1.27.3) was discovered by Sato and Egami. Ando discovered Aspergillus nuclease S1 (single-stranded nucleate endonuclease, EC 3.1.30.1). Aspergillopepsin I (EC 3.4.23.18) from A. tubingensis (formerly designated as A. saitoi) activates trypsinogen to trypsin. Shintani et al. demonstrated Asp76 of aspergillopepsin I as the binding site for the basic substrate, trypsinogen. The new oligosaccharide moieties Man10GlcNAc2 and Man11GlcNAc2 were identified with α-1,2-mannosidase (EC 3.2.1.113) from A. tubingensis. A yeast mutant compatible of producing Man5GlcNAc2 human compatible sugar chains on glycoproteins was constructed. The acid activation of protyrosinase from A. oryzae at pH 3.0 was resolved. The hyper-protein production system of glucoamylase was established in a submerged culture.

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“…This step acts as quality control system of the glycoproteins before transporting them to the Golgi apparatus, as studied in A. oryzae (Watanabe et al 2009 , 2007 ). Thereafter, a sequential cleavage of mannose moieties by two 1,2-α-mannosidases (ManE and FmanIB) occurs at the ER and the Golgi apparatus as well, also studied in A. oryzae (Yoshida et al 2000 ; Akao et al 2006 , 2012 ). The remaining Man 6 GlcNAc 2 moiety is a secretory form of the N -glycan chain (Fig.…”

Section: Protein Secretionmentioning

confidence: 99%

Protein secretion and associated stress in industrially employed filamentous fungi

Jadhav,

Mach,

Mach-Aigner

2024

Appl Microbiol Biotechnol

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Application of filamentous fungi for the production of commercial enzymes such as amylase, cellulase, or xylanase is on the rise due to the increasing demand to degrade several complex carbohydrates as raw material for biotechnological processes. Also, protein production by fungi for food and feed gains importance. In any case, the protein production involves both cellular synthesis and secretion outside of the cell. Unfortunately, the secretion of proteins or enzymes can be hampered due to accumulation of unfolded or misfolded proteins in the endoplasmic reticulum (ER) as a result of too high synthesis of enzymes or (heterologous) protein expression. To cope with this ER stress, the cell generates a response known as unfolded protein response (UPR). Even though this mechanism should re-establish the protein homeostasis equivalent to a cell under non-stress conditions, the enzyme expression might still suffer from repression under secretory stress (RESS). Among eukaryotes, Saccharomyces cerevisiae is the only fungus, which is studied quite extensively to unravel the UPR pathway. Several homologs of the proteins involved in this signal transduction cascade are also found in filamentous fungi. Since RESS seems to be absent in S. cerevisiae and was only reported in Trichoderma reesei in the presence of folding and glycosylation inhibitors such as dithiothreitol and tunicamycin, more in-depth study about this mechanism, specifically in filamentous fungi, is the need of the hour. Hence, this review article gives an overview on both, protein secretion and associated stress responses in fungi. Key points • Enzymes produced by filamentous fungi are crucial in industrial processes • UPR mechanism is conserved among many fungi, but mediated by different proteins • RESS is not fully understood or studied in industrially relevant filamentous fungi

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Lack of endoplasmic reticulum 1,2-α-mannosidase activity that trims N-glycan Man9GlcNAc2 to Man8GlcNAc2 isomer B in a manE gene disruptant of Aspergillus oryzae

Cited by 7 publications

References 11 publications

Genome sequence ofAspergillus luchuensisNBRC 4314

Genome sequence ofAspergillus luchuensisNBRC 4314

Development of enzyme technology for Aspergillus oryzae, A. sojae, and A. luchuensis,the national microorganisms of Japan

Protein secretion and associated stress in industrially employed filamentous fungi

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