ネオカリマスティクス属、Neocallimastix属
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- Neocallimasticales
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/08/06 12:05:35」(JST)
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A specialised group of chytrids grow in the rumen of herbivorous animals, where they degrade cellulose and thus play a primary role in the complex microbial ecology of the rumen.
Neocallimastix |
Scientific classification |
Kingdom: |
Fungi |
Division: |
Neocallimastigomycota |
Class: |
Neocallimastigomycetes |
Order: |
Neocallimastigales |
Family: |
Neocallimastigaceae |
Genus: |
Neocallimastix
Vavra & Joyon ex I.B.Heath (1983)[1] |
Type species |
Neocallimastix frontalis
(R.A.Braune) Vavra & Joyon ex I.B.Heath (1983) |
Species |
N. frontalis
N. hurleyensis
N. joyoni
N. patriciarum
N. variabilis
|
Neocallimastix is a genus of obligately anaerobic rumen fungi in the family Neocallimastigaceae.[2]
References
- ^ Heath IB, Bauchop T, Skipp RA. (1983). "Assignment of the rumen anaerobe Neocallimastix frontalis to the Spizellomycetales (Chytridiomycetes) on the basis of its polyflagellate zoospore ultrastructure". Canadian Journal of Botany 61 (1): 295–307. doi:10.1139/b83-033.
- ^ Carlile MJ, Watkinson SC. (1994). The Fungi. Academic Press. pp. 33–34. ISBN 0-12-159960-4.
External links
- Neocallimastix in Index Fungorum.
English Journal
- Finding a robust strain for biomethanation: Anaerobic fungi (Neocallimastigomycota) from the Alpine ibex (Capra ibex) and their associated methanogens.
- Leis S1, Dresch P1, Peintner U1, Fliegerová K2, Sandbichler AM3, Insam H1, Podmirseg SM4.Author information 1Institute of Microbiology, University of Innsbruck, Technikerstraße 25d, A-6020 Innsbruck, Austria.2Institute of Animal Physiology and Genetics, Czech Academy of Sciences, Videnska 1083, Prague, Czech Republic.3Institute of Zoology, University of Innsbruck, Technikerstraße 25, A-6020 Innsbruck, Austria.4Institute of Microbiology, University of Innsbruck, Technikerstraße 25d, A-6020 Innsbruck, Austria. Electronic address: sabine.podmirseg@uibk.ac.at.AbstractAnaerobic fungi occupy the rumen and digestive tract of herbivores, where they play an important role in enzymatic digestion of lignocellulosic and cellulosic substrates, i.e. organic material that their hosts are unable to decompose on their own. In this study we isolated anaerobic fungi from a typical alpine herbivore, the Alpine ibex (C. ibex). Three fungal strains, either as pure culture (ST2) or syntrophic co-culture with methanogens (ST3, ST4) were successfully obtained and morphologically characterised by different microscopy- and staining-techniques and by rDNA ITS gene sequencing. The isolated fungi were identified as Neocallimastix frontalis (ST2) and Caecomyces communis (ST3 and ST4). We introduce a novel field of application for lactofuchsin-staining, combined with confocal laser scanning microscopy. This approach proved as an effective method to visualize fungal structures, especially in the presence of plant biomass, generally exhibiting high autofluorescence. Moreover, we could demonstrate that fungal morphology is subject to changes depending on the carbon source used for cultivation. Oxygen tolerance was confirmed for both, C. communis-cultures for up to three, and for the N. frontalis-isolate for up to 12 h, respectively. With PCR, FISH and an oligonucleotide microarray we found associated methanogens (mainly Methanobacteriales) for C. communis, but not for N. frontalis.
- Anaerobe.Anaerobe.2013 Dec 30. pii: S1075-9964(13)00208-4. doi: 10.1016/j.anaerobe.2013.12.002. [Epub ahead of print]
- Anaerobic fungi occupy the rumen and digestive tract of herbivores, where they play an important role in enzymatic digestion of lignocellulosic and cellulosic substrates, i.e. organic material that their hosts are unable to decompose on their own. In this study we isolated anaerobic fungi from a typ
- PMID 24384307
- Highly divergent mitochondrion-related organelles in anaerobic parasitic protozoa.
- Makiuchi T1, Nozaki T2.Author information 1Department of Infectious Diseases, Tokai University School of Medicine, Isehara, Kanagawa 259-1193, Japan; Department of Parasitology, National Institute of Infectious Diseases, 1-23-1 Toyama, Shinjuku-ku, Tokyo 162-8640, Japan.2Department of Parasitology, National Institute of Infectious Diseases, 1-23-1 Toyama, Shinjuku-ku, Tokyo 162-8640, Japan; Graduate School of Life and Environmental Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8572, Japan. Electronic address: nozaki@nih.go.jp.AbstractThe mitochondria have arisen as a consequence of endosymbiosis of an ancestral α-proteobacterium with a methane-producing archae. The main function of the canonical aerobic mitochondria include ATP generation via oxidative phosphorylation, heme and phospholipid synthesis, calcium homeostasis, programmed cell death, and the formation of iron-sulfur clusters. Under oxygen-restricted conditions, the mitochondrion has often undergone remarkable reductive alterations of its content and function, leading to the generation of mitochondrion-related organelles (MROs), such as mitosomes, hydrogenosomes, and mithochondrion-like organelles, which are found in a wide range of anaerobic/microaerophilic eukaryotes that include several medically important parasitic protists such as Entamoeba histolytica, Giardia intestinalis, Trichomonas vaginalis, Cryptosporidium parvum, Blastocystis hominis, and Encephalitozoon cuniculi, as well as free-living protists such as Sawyeria marylandensis, Neocallimastix patriciarum, and Mastigamoeba balamuthi. The transformation from canonical aerobic mitochondria to MROs apparently have occurred in independent lineages, and resulted in the diversity of their components and functions. Due to medical and veterinary importance of the MRO-possessing human- and animal-pathogenic protozoa, their genomic, transcriptomic, proteomic, and biochemical evidence has been accumulated. Detailed analyses of the constituents and functions of the MROs in such anaerobic pathogenic protozoa, which reside oxygen-deprived or oxygen-poor environments such as the mammalian intestine and the genital organs, should illuminate the current evolutionary status of the MROs in these organisms, and give insight to environmental constraints that drive the evolution of eukaryotes and their organelles. In this review, we summarize and discuss the diverse metabolic functions and protein transport systems of the MROs from anaerobic parasitic protozoa.
- Biochimie.Biochimie.2013 Dec 4. pii: S0300-9084(13)00427-6. doi: 10.1016/j.biochi.2013.11.018. [Epub ahead of print]
- The mitochondria have arisen as a consequence of endosymbiosis of an ancestral α-proteobacterium with a methane-producing archae. The main function of the canonical aerobic mitochondria include ATP generation via oxidative phosphorylation, heme and phospholipid synthesis, calcium homeostasis, progr
- PMID 24316280
- Cloning and characterization of a thermostable and pH-stable cellobiohydrolase from Neocallimastix patriciarum J11.
- Wang HC, Chen YC, Huang CT, Hseu RS.Author information Department of Biochemical Science and Technology, National Taiwan University, Taipei, Taiwan.AbstractAn 1888-bp cDNA designated celA, isolated from a cDNA library of Neocallimastix patriciarum J11 was cloned. The celA had an open reading frame of 1530 bp encoding J11 CelA of 510 amino acids. The primary structure analysis of J11 CelA revealed a complete cellulose-binding domain at the N-terminal, followed by an Asn, Ala, Gly, Gln and Pro-rich linker and ending with a C-terminal glycosyl hydrolase family 6 catalytic domain. The mature J11 CelA was overexpressed in Escherichia coli and purified to homogeneity. This enzyme had high specific activities towards barley β-glucan and lichenan, low toward carboxymethyl cellulose (CMC), Avicel, and H3PO4-swollen Avicel (PSA). The product of Avicel hydrolysis was cellobiose indicating that J11 CelA is a typical cellobiohydrolase. The recombinant J11 CelA had an optimal pH of 6.0 and was stable over a wide range of pH (5.2-11.3). The enzyme showed an optimal temperature of 50°C and was still maintained approximately 50% of the maximum activity in response to the treatment at 70°C for 1h. Cobalt and Fe(3+) at 1 mM greatly activated the enzyme activity. As a thermostable and pH stable enzyme with crystalline cellulose-degrading activity, J11 CelA is a potential candidate for the bioethanol industry.
- Protein expression and purification.Protein Expr Purif.2013 Aug;90(2):153-9. doi: 10.1016/j.pep.2013.06.004. Epub 2013 Jun 13.
- An 1888-bp cDNA designated celA, isolated from a cDNA library of Neocallimastix patriciarum J11 was cloned. The celA had an open reading frame of 1530 bp encoding J11 CelA of 510 amino acids. The primary structure analysis of J11 CelA revealed a complete cellulose-binding domain at the N-terminal, f
- PMID 23770555
Japanese Journal
- Efficient Production of Cellulolytic and Xylanolytic Enzymes by the Rumen Anaerobic Fungus, Neocallimastix frontalis, in a Repeated Batch Culture
- Srinivasan Karthikeyan,Murakami Makoto,Nakashimada Yutaka [他],NISHIO NAOMICHI
- Journal of bioscience and bioengineering 91(2), 153-158, 2001-02-25
- … In a batch culture of Neocallimastix frontalis in a medium (pH 6.8) containing 8 g・l^<-1> …
- NAID 110002683800
- Expression of a modified Neocallimastix partriciarum xylanase in Butyrivibrio fibrisolvens digests more fibre but can not effectively compete with highly fibrolytic bacteria in the rumen
- 942 偏性嫌気性糸状菌Neocallimastix frontalisと水素生産菌との共生培養によるバイオマスからの直接水素生産
Related Links
- Classification Higher Order Taxa- Eukaryota; Fungi; Neocallimastigaceae; Neocallimastix Species- N. frontalis, N.hurleyensis, N. joyonii, N. patriciarum, N. variabilis, N. sp. AF-CTS-2G, N.sp. AF-CTS-BF-2, N. sp. GE13, N. sp ...
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