Author Report for: Gomi KNo contact information in database for Gomi K
Yoshimi A, Yamaguchi S, Fujioka T, Kawai K, Gomi K, Machida M, Abe K Ref: Front Microbiol, 9:690, 2018 : PubMed ESTHER: Yoshimi_2018_Front.Microbiol_9_690 PubMedSearch: Yoshimi 2018 Front.Microbiol 9 690 PubMedID: 29686660 Gene_locus related to this paper: curcl-tr09 Abstract A novel cyclic peptide compound, KK-1, was originally isolated from the plant-pathogenic fungus Curvularia clavata. It consists of 10 amino acid residues, including five N-methylated amino acid residues, and has potent antifungal activity. Recently, the genome-sequencing analysis of C. clavata was completed, and the biosynthetic genes involved in KK-1 production were predicted by using a novel gene cluster mining tool, MIDDAS-M. These genes form an approximately 75-kb cluster, which includes nine open reading frames, containing a non-ribosomal peptide synthetase (NRPS) gene. To determine whether the predicted genes were responsible for the biosynthesis of KK-1, we performed heterologous production of KK-1 in Aspergillus oryzae by introduction of the cluster genes into the genome of A. oryzae. The NRPS gene was split in two fragments and then reconstructed in the A. oryzae genome, because the gene was quite large (approximately 40 kb). The remaining seven genes in the cluster, excluding the regulatory gene kkR, were simultaneously introduced into the strain of A. oryzae in which NRPS had already been incorporated. To evaluate the heterologous production of KK-1 in A. oryzae, gene expression was analyzed by RT-PCR and KK-1 productivity was quantified by HPLC. KK-1 was produced in variable quantities by a number of transformed strains, along with expression of the cluster genes. The amount of KK-1 produced by the strain with the greatest expression of all genes was lower than that produced by the original producer, C. clavata. Therefore, expression of the cluster genes is necessary and sufficient for the heterologous production of KK-1 in A. oryzae, although there may be unknown factors limiting productivity in this species. Title: Increased enzyme production under liquid culture conditions in the industrial fungus Aspergillus oryzae by disruption of the genes encoding cell wall alpha-1,3-glucan synthase Miyazawa K, Yoshimi A, Zhang S, Sano M, Nakayama M, Gomi K, Abe K Ref: Biosci Biotechnol Biochem, :1, 2016 : PubMed ESTHER: Miyazawa_2016_Biosci.Biotechnol.Biochem__1 PubMedSearch: Miyazawa 2016 Biosci.Biotechnol.Biochem 1 PubMedID: 27442340 Abstract Under liquid culture conditions, the hyphae of filamentous fungi aggregate to form pellets, which reduces cell density and fermentation productivity. Previously, we found that loss of alpha-1,3-glucan in the cell wall of the fungus Aspergillus nidulans increased hyphal dispersion. Therefore, here we constructed a mutant of the industrial fungus A. oryzae in which the three genes encoding alpha-1,3-glucan synthase were disrupted (tripleDelta). Although the hyphae of the tripleDelta mutant were not fully dispersed, the mutant strain did form smaller pellets than the wild-type strain. We next examined enzyme productivity under liquid culture conditions by transforming the cutinase-encoding gene cutL1 into A. oryzae wild-type and the tripleDelta mutant (i.e. wild-type-cutL1, tripleDelta-cutL1). A. oryzae tripleDelta-cutL1 formed smaller hyphal pellets and showed both greater biomass and increased CutL1 productivity compared with wild-type-cutL1, which might be attributable to a decrease in the number of tripleDelta-cutL1 cells under anaerobic conditions. Title: Genome sequence of Aspergillus luchuensis NBRC 4314 Yamada O, Machida M, Hosoyama A, Goto M, Takahashi T, Futagami T, Yamagata Y, Takeuchi M, Kobayashi T and Gomi K <17 more author(s)> Yamada O, Machida M, Hosoyama A, Goto M, Takahashi T, Futagami T, Yamagata Y, Takeuchi M, Kobayashi T, Koike H, Abe K, Asai K, Arita M, Fujita N, Fukuda K, Higa KI, Horikawa H, Ishikawa T, Jinno K, Kato Y, Kirimura K, Mizutani O, Nakasone K, Sano M, Shiraishi Y, Tsukahara M, Gomi K (- 17) Ref: DNA Research, 23:507, 2016 : PubMed ESTHER: Yamada_2016_DNA.Res_23_507 PubMedSearch: Yamada 2016 DNA.Res 23 507 PubMedID: 27651094 Gene_locus related to this paper: 9euro-a0a146f3d2 Abstract 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 alpha-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. Title: Aspergillus luchuensis, an industrially important black Aspergillus in East Asia Hong SB, Lee M, Kim DH, Varga J, Frisvad JC, Perrone G, Gomi K, Yamada O, Machida M and Samson RA <1 more author(s)> Hong SB, Lee M, Kim DH, Varga J, Frisvad JC, Perrone G, Gomi K, Yamada O, Machida M, Houbraken J, Samson RA (- 1) Ref: PLoS ONE, 8:e63769, 2013 : PubMed ESTHER: Hong_2013_PLoS.One_8_e63769 PubMedSearch: Hong 2013 PLoS.One 8 e63769 PubMedID: 23723998 Gene_locus related to this paper: aspaw-AXE1 Abstract Aspergilli known as black- and white-koji molds which are used for awamori, shochu, makgeolli and other food and beverage fermentations, are reported in the literature as A. luchuensis, A. awamori, A. kawachii, or A. acidus. In order to elucidate the taxonomic position of these species, available ex-type cultures were compared based on morphology and molecular characters. A. luchuensis, A. kawachii and A. acidus showed the same banding patterns in RAPD, and the three species had the same rDNA-ITS, beta-tubulin and calmodulin sequences and these differed from those of the closely related A. niger and A. tubingensis. Morphologically, the three species are not significantly different from each other or from A. niger and A. tubingensis. It is concluded that A. luchuensis, A. kawachii and A. acidus are the same species, and A. luchuensis is selected as the correct name based on priority. Strains of A. awamori which are stored in National Research Institute of Brewing in Japan, represent A. niger (n = 14) and A. luchuensis (n = 6). The neotype of A. awamori (CBS 557.65 = NRRL 4948) does not originate from awamori fermentation and it is shown to be identical with the unknown taxon Aspergillus welwitschiae. Extrolite analysis of strains of A. luchuensis showed that they do not produce mycotoxins and therefore can be considered safe for food and beverage fermentations. A. luchuensis is also frequently isolated from meju and nuruk in Korea and Puerh tea in China and the species is probably common in the fermentation environment of East Asia. A re-description of A. luchuensis is provided because the incomplete data in the original literature. Title: Functional analysis of FarA transcription factor in the regulation of the genes encoding lipolytic enzymes and hydrophobic surface binding protein for the degradation of biodegradable plastics in Aspergillus oryzae Garrido SM, Kitamoto N, Watanabe A, Shintani T, Gomi K Ref: J Biosci Bioeng, 113:549, 2012 : PubMed ESTHER: Garrido_2012_J.Biosci.Bioeng_113_549 PubMedSearch: Garrido 2012 J.Biosci.Bioeng 113 549 PubMedID: 22280964 Abstract FarA is a Zn(II)(2)Cys(6) transcription factor which upregulates genes required for growth on fatty acids in filamentous fungi like Aspergillus nidulans. FarA is also highly similar to the cutinase transcription factor CTF1 alpha of Fusarium solani which binds to the cutinase gene promoter in this plant pathogen. This study determines whether FarA transcriptional factor also works in the regulation of genes responsible for the production of cutinase for the degradation of a biodegradable plastic, poly-(butylene succinate-co-adipate) (PBSA), in Aspergillus oryzae. The wild-type and the farA gene disruption strains were grown in minimal agar medium with emulsified PBSA, and the wild-type showed clear zone around the colonies while the disruptants did not. Western blot analysis revealed that the cutinase protein CutL1 and a hydrophobic surface binding protein such as HsbA were produced by the wild-type but not by the disruptants. In addition, the expressions of cutL1, triacylglycerol lipase (tglA), and mono- and di-acylglycerol lipase (mdlB) genes as well as the hsbA gene were significantly lower in the disruptants compared to the wild-type. These results indicated that the FarA transcriptional factor would be implicated in the expression of cutL1 and hsbA genes that are required for the degradation of PBSA as well as lipolytic genes such as mdlB and tglA for lipid hydrolysis. Title: Role of the host-selective ACT-toxin synthesis gene ACTTS2 encoding an enoyl-reductase in pathogenicity of the tangerine pathotype of Alternaria alternata Ajiro N, Miyamoto Y, Masunaka A, Tsuge T, Yamamoto M, Ohtani K, Fukumoto T, Gomi K, Peever TL and Akimitsu K <2 more author(s)> Ajiro N, Miyamoto Y, Masunaka A, Tsuge T, Yamamoto M, Ohtani K, Fukumoto T, Gomi K, Peever TL, Izumi Y, Tada Y, Akimitsu K (- 2) Ref: Phytopathology, 100:120, 2010 : PubMed ESTHER: Ajiro_2010_Phytopathology_100_120 PubMedSearch: Ajiro 2010 Phytopathology 100 120 PubMedID: 20055645 Gene_locus related to this paper: altal-actt2 Abstract ABSTRACT The tangerine pathotype of Alternaria alternata produces host-selective ACT-toxin and causes Alternaria brown spot disease of tangerines and tangerine hybrids. Sequence analysis of a genomic BAC clone identified a previously uncharacterized portion of the ACT-toxin biosynthesis gene cluster (ACTT). A 1,034-bp gene encoding a putative enoyl-reductase was identified by using rapid amplification of cDNA ends and polymerase chain reaction and designated ACTTS2. Genomic Southern blots demonstrated that ACTTS2 is present only in ACT-toxin producers and is carried on a 1.9 Mb conditionally dispensable chromosome by the tangerine pathotype. Targeted gene disruption of ACTTS2 led to a reduction in ACT-toxin production and pathogenicity, and transcriptional knockdown of ACTTS2 using RNA silencing resulted in complete loss of ACT-toxin production and pathogenicity. These results indicate that ACTTS2 is an essential gene for ACT-toxin biosynthesis in the tangerine pathotype of A. alternata and is required for pathogenicity of this fungus. Title: ACTTS3 encoding a polyketide synthase is essential for the biosynthesis of ACT-toxin and pathogenicity in the tangerine pathotype of Alternaria alternata Miyamoto Y, Masunaka A, Tsuge T, Yamamoto M, Ohtani K, Fukumoto T, Gomi K, Peever TL, Tada Y and Akimitsu K <1 more author(s)> Miyamoto Y, Masunaka A, Tsuge T, Yamamoto M, Ohtani K, Fukumoto T, Gomi K, Peever TL, Tada Y, Ichimura K, Akimitsu K (- 1) Ref: Mol Plant Microbe Interact, 23:406, 2010 : PubMed ESTHER: Miyamoto_2010_Mol.Plant.Microbe.Interact_23_406 PubMedSearch: Miyamoto 2010 Mol.Plant.Microbe.Interact 23 406 PubMedID: 20192828 Gene_locus related to this paper: altal-actt2 Abstract The tangerine pathotype of Alternaria alternata produces host-selective ACT-toxin and causes Alternaria brown spot disease of tangerine and tangerine hybrids. Sequence analysis of a genomic BAC clone identified part of the ACT-toxin TOX (ACTT) gene cluster, and knockout experiments have implicated several open reading frames (ORF) contained within the cluster in the biosynthesis of ACT-toxin. One of the ORF, designated ACTTS3, encoding a putative polyketide synthase, was isolated by rapid amplification of cDNA ends and genomic/reverse transcription-polymerase chain reactions using the specific primers designed from the BAC sequences. The 7,374-bp ORF encodes a polyketide synthase with putative beta-ketoacyl synthase, acyltransferase, methyltransferase, beta-ketoacyl reductase, and phosphopantetheine attachment site domains. Genomic Southern blots demonstrated that ACTTS3 is present on the smallest chromosome in the tangerine pathotype of A. alternata, and the presence of ACTTS3 is highly correlated with ACT-toxin production and pathogenicity. Targeted gene disruption of two copies of ACTTS3 led to a complete loss of ACT-toxin production and pathogenicity. These results indicate that ACTTS3 is an essential gene for ACT-toxin biosynthesis in the tangerine pathotype of A. alternata and is required for pathogenicity of this fungus. Title: Function of genes encoding acyl-CoA synthetase and enoyl-CoA hydratase for host-selective act-toxin biosynthesis in the tangerine pathotype of Alternaria alternata Miyamoto Y, Ishii Y, Honda A, Masunaka A, Tsuge T, Yamamoto M, Ohtani K, Fukumoto T, Gomi K and Akimitsu K <1 more author(s)> Miyamoto Y, Ishii Y, Honda A, Masunaka A, Tsuge T, Yamamoto M, Ohtani K, Fukumoto T, Gomi K, Peever TL, Akimitsu K (- 1) Ref: Phytopathology, 99:369, 2009 : PubMed ESTHER: Miyamoto_2009_Phytopathology_99_369 PubMedSearch: Miyamoto 2009 Phytopathology 99 369 PubMedID: 19271978 Gene_locus related to this paper: altal-actt2 Abstract The tangerine pathotype of Alternaria alternata produces host-selective ACT-toxin and causes Alternaria brown spot disease. Sequence analysis of a genomic cosmid clone identified a part of the ACTT gene cluster and implicated two genes, ACTT5 encoding an acyl-CoA synthetase and ACTT6 encoding an enoyl-CoA hydratase, in the biosynthesis of ACT-toxin. Genomic Southern blots demonstrated that both genes were present in tangerine pathotype isolates producing ACT-toxin and also in Japanese pear pathotype isolates producing AK-toxin and strawberry pathotype isolates producing AF-toxin. ACT-, AK-, and AF-toxins from these three pathotypes share a common 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid moiety. Targeted gene disruption of two copies of ACTT5 significantly reduced ACT-toxin production and virulence. Targeted gene disruption of two copies of ACTT6 led to complete loss of ACT-toxin production and pathogenicity and a putative decatrienoic acid intermediate in ACT-toxin biosynthesis accumulated in mycelial mats. These results indicate that ACTT5 and ACTT6 are essential genes in ACT-toxin biosynthesis in the tangerine pathotype of A. alternata and both are required for full virulence of this fungus. Title: Genomics of Aspergillus oryzae: learning from the history of Koji mold and exploration of its future Machida M, Yamada O, Gomi K Ref: DNA Research, 15:173, 2008 : PubMed ESTHER: Machida_2008_DNA.Res_15_173 PubMedSearch: Machida 2008 DNA.Res 15 173 PubMedID: 18820080 Abstract At a time when the notion of microorganisms did not exist, our ancestors empirically established methods for the production of various fermentation foods: miso (bean curd seasoning) and shoyu (soy sauce), both of which have been widely used and are essential for Japanese cooking, and sake, a magical alcoholic drink consumed at a variety of ritual occasions, are typical examples. A filamentous fungus, Aspergillus oryzae, is the key organism in the production of all these traditional foods, and its solid-state cultivation (SSC) has been confirmed to be the secret for the high productivity of secretory hydrolases vital for the fermentation process. Indeed, our genome comparison and transcriptome analysis uncovered mechanisms for effective degradation of raw materials in SSC: the extracellular hydrolase genes that have been found only in the A. oryzae genome but not in A. fumigatus are highly induced during SSC but not in liquid cultivation. Also, the temperature reduction process empirically adopted in the traditional soy-sauce fermentation processes has been found to be important to keep strong expression of the A. oryzae-specific extracellular hydrolases. One of the prominent potentials of A. oryzae is that it has been successfully applied to effective degradation of biodegradable plastic. Both cutinase, responsible for the degradation of plastic, and hydrophobin, which recruits cutinase on the hydrophobic surface to enhance degradation, have been discovered in A. oryzae. Genomic analysis in concert with traditional knowledge and technology will continue to be powerful tools in the future exploration of A. oryzae. Title: Functional analysis of a multicopy host-selective ACT-toxin biosynthesis gene in the tangerine pathotype of Alternaria alternata using RNA silencing Miyamoto Y, Masunaka A, Tsuge T, Yamamoto M, Ohtani K, Fukumoto T, Gomi K, Peever TL, Akimitsu K Ref: Mol Plant Microbe Interact, 21:1591, 2008 : PubMed ESTHER: Miyamoto_2008_Mol.Plant.Microbe.Interact_21_1591 PubMedSearch: Miyamoto 2008 Mol.Plant.Microbe.Interact 21 1591 PubMedID: 18986255 Gene_locus related to this paper: altal-aft8, altal-actt2 Abstract Alternaria brown spot, caused by the tangerine pathotype of Alternaria alternata, is a serious disease of commercially important tangerines and their hybrids. The pathogen produces host-selective ACT toxin, and several genes (named ACTT) responsible for ACT-toxin biosynthesis have been identified. These genes have many paralogs, which are clustered on a small, conditionally dispensable chromosome, making it difficult to disrupt entire functional copies of ACTT genes using homologous recombination-mediated gene disruption. To overcome this problem, we attempted to use RNA silencing, which has never been employed in Alternaria spp., to knock down the functional copies of one ACTT gene with a single silencing event. ACTT2, which encodes a putative hydrolase and is present in multiple copies in the genome, was silenced by transforming the fungus with a plasmid construct expressing hairpin ACTT2 RNAs. The ACTT2 RNA-silenced transformant (S-7-24-2) completely lost ACTT2 transcripts and ACT-toxin production as well as pathogenicity. These results indicated that RNA silencing may be a useful technique for studying the role of ACTT genes responsible for host-selective toxin biosynthesis in A. alternata. Further, this technique may be broadly applicable to the analysis of many genes present in multiple copies in fungal genomes that are difficult to analyze using recombination-mediated knockdowns. Title: Genome sequencing and analysis of Aspergillus oryzae Machida M, Asai K, Sano M, Tanaka T, Kumagai T, Terai G, Kusumoto K, Arima T, Akita O and Kikuchi H <54 more author(s)> Machida M, Asai K, Sano M, Tanaka T, Kumagai T, Terai G, Kusumoto K, Arima T, Akita O, Kashiwagi Y, Abe K, Gomi K, Horiuchi H, Kitamoto K, Kobayashi T, Takeuchi M, Denning DW, Galagan JE, Nierman WC, Yu J, Archer DB, Bennett JW, Bhatnagar D, Cleveland TE, Fedorova ND, Gotoh O, Horikawa H, Hosoyama A, Ichinomiya M, Igarashi R, Iwashita K, Juvvadi PR, Kato M, Kato Y, Kin T, Kokubun A, Maeda H, Maeyama N, Maruyama J, Nagasaki H, Nakajima T, Oda K, Okada K, Paulsen I, Sakamoto K, Sawano T, Takahashi M, Takase K, Terabayashi Y, Wortman JR, Yamada O, Yamagata Y, Anazawa H, Hata Y, Koide Y, Komori T, Koyama Y, Minetoki T, Suharnan S, Tanaka A, Isono K, Kuhara S, Ogasawara N, Kikuchi H (- 54) Ref: Nature, 438:1157, 2005 : PubMed ESTHER: Machida_2005_Nature_438_1157 PubMedSearch: Machida 2005 Nature 438 1157 PubMedID: 16372010 Gene_locus related to this paper: aspor-Q2U722, aspfn-b8mvx2, aspfn-b8mwk1, aspfn-b8n1a4, aspfn-b8n5l3, aspfn-b8n7y0, aspfn-b8n829, aspfn-b8ncj5, aspfn-b8nhj9, aspfn-b8njx6, aspfn-b8nsk2, aspfu-q4wj61, aspor-axe1, aspor-CPI, aspor-cutas, aspor-cuti2, aspor-DPPIV, aspor-faec, aspor-MDLB, aspor-ppme1, aspor-q2tw11, aspor-q2tw16, aspor-q2tw28, aspor-q2twc4, aspor-q2twg0, aspor-q2twj3, aspor-q2twv2, aspor-q2twv4, aspor-q2tx21, aspor-q2txq8, aspor-q2tya1, aspor-q2tyh6, aspor-q2tyn9, aspor-q2typ0, aspor-q2tyq4, aspor-q2tyv8, aspor-q2tz03, aspor-q2tzh3, aspor-q2tzr5, aspor-q2tzv9, aspor-q2u0k7, aspor-q2u0q2, aspor-q2u0r6, aspor-q2u1a5, aspor-q2u1a6, aspor-q2u1k0, aspor-q2u1k8, aspor-q2u1m8, aspor-q2u2a1, aspor-q2u2a4, aspor-q2u3a3, aspor-q2u3a6, aspor-q2u3k5, aspor-q2u3l6, aspor-q2u4a0, aspor-q2u4e0, aspor-q2u4f6, aspor-q2u4g6, aspor-q2u4h9, aspor-q2u4w9, aspor-q2u4y8, aspor-q2u5f5, aspor-q2u5n3, aspor-q2u5y8, aspor-q2u6h7, aspor-q2u6j5, aspor-q2u6m8, aspor-q2u6m9, aspor-q2u6n6, aspor-q2u7i2, aspor-q2u7v0, aspor-q2u8j8, aspor-q2u8r1, aspor-q2u8r4, aspor-q2u8t5, aspor-q2u8z3, aspor-q2u9a1, aspor-q2u9n5, aspor-q2u144, aspor-q2u161, aspor-q2u185, aspor-q2u199, aspor-q2u212, aspor-q2u331, aspor-q2u348, aspor-q2u400, aspor-q2u453, aspor-q2u489, aspor-q2u704, aspor-q2u728, aspor-q2u798, aspor-q2u822, aspor-q2u854, aspor-q2u875, aspor-q2u908, aspor-q2ua10, aspor-q2ua48, aspor-q2uab6, aspor-q2uak9, aspor-q2uaq4, aspor-q2ub32, aspor-q2ub76, aspor-q2uba1, aspor-q2ubd6, aspor-q2ubm2, aspor-q2ubr2, aspor-q2uc28, aspor-q2uc65, aspor-q2uc77, aspor-q2uc98, aspor-q2uck0, aspor-q2ucy7, aspor-q2ud03, aspor-q2ud06, aspor-q2ud08, aspor-q2ud23, aspor-q2udn5, aspor-q2udr0, aspor-q2uec1, aspor-q2uef3, aspor-q2uf10, aspor-q2uf27, aspor-q2uf48, aspor-q2ufd8, aspor-q2ufe5, aspor-q2ufm4, aspor-q2ufr3, aspor-q2ufz8, aspor-q2ug78, aspor-q2ugd6, aspor-q2uge1, aspor-q2ugg7, aspor-q2ugi2, aspor-q2ugl2, aspor-q2ugy9, aspor-q2uh24, aspor-q2uh73, aspor-q2uhe4, aspor-q2uhf0, aspor-q2uhj6, aspor-q2uhn1, aspor-q2uhq0, aspor-q2ui56, aspor-q2uib2, aspor-q2uib5, aspor-q2uie9, aspor-q2uih1, aspor-q2uii1, aspor-q2uik9, aspor-q2uiq0, aspor-q2uiu1, aspor-q2uix9, aspor-q2uiy5, aspor-q2uiz4, aspor-q2uj89, aspor-q2uja2, aspor-q2uju3, aspor-q2uk31, aspor-q2uk42, aspor-q2ukb6, aspor-q2ukq7, aspor-q2ul81, aspor-q2uli9, aspor-q2ulr2, aspor-q2ulv7, aspor-q2umf3, aspor-q2umv2, aspor-q2umx6, aspor-q2unw5, aspor-q2up23, aspor-q2up89, aspor-q2upe6, aspor-q2upi1, aspor-q2upl1, aspor-q2upw4, aspor-q2uq56, aspor-q2uqb4, aspor-q2uqm7, aspor-q2ur58, aspor-q2ur64, aspor-q2ur80, aspor-q2ur83, aspor-q2ure7, aspor-q2urf3, aspor-q2urg5, aspor-q2urq0, aspor-q2urt4, aspor-q2uru5, aspor-q2usi0, aspor-q2usp7, aspor-q2usq8, aspor-q2usv6, aspor-q2uta5, aspor-q2uu89, aspor-q2uub4, aspor-q2uux8, aspor-q2uv29, aspor-TGLA, aspor-q2ue03, aspor-q2uj83, aspno-a0a0l1j1c9 Abstract The genome of Aspergillus oryzae, a fungus important for the production of traditional fermented foods and beverages in Japan, has been sequenced. The ability to secrete large amounts of proteins and the development of a transformation system have facilitated the use of A. oryzae in modern biotechnology. Although both A. oryzae and Aspergillus flavus belong to the section Flavi of the subgenus Circumdati of Aspergillus, A. oryzae, unlike A. flavus, does not produce aflatoxin, and its long history of use in the food industry has proved its safety. Here we show that the 37-megabase (Mb) genome of A. oryzae contains 12,074 genes and is expanded by 7-9 Mb in comparison with the genomes of Aspergillus nidulans and Aspergillus fumigatus. Comparison of the three aspergilli species revealed the presence of syntenic blocks and A. oryzae-specific blocks (lacking synteny with A. nidulans and A. fumigatus) in a mosaic manner throughout the genome of A. oryzae. The blocks of A. oryzae-specific sequence are enriched for genes involved in metabolism, particularly those for the synthesis of secondary metabolites. Specific expansion of genes for secretory hydrolytic enzymes, amino acid metabolism and amino acid/sugar uptake transporters supports the idea that A. oryzae is an ideal microorganism for fermentation. Title: Purification and characterization of a biodegradable plastic-degrading enzyme from Aspergillus oryzae Maeda H, Yamagata Y, Abe K, Hasegawa F, Machida M, Ishioka R, Gomi K, Nakajima T Ref: Applied Microbiology & Biotechnology, 67:778, 2005 : PubMed ESTHER: Maeda_2005_Appl.Microbiol.Biotechnol_67_778 PubMedSearch: Maeda 2005 Appl.Microbiol.Biotechnol 67 778 PubMedID: 15968570 Gene_locus related to this paper: aspor-cutas Abstract We used biodegradable plastics as fermentation substrates for the filamentous fungus Aspergillus oryzae. This fungus could grow under culture conditions that contained emulsified poly-(butylene succinate) (PBS) and emulsified poly-(butylene succinate-co-adipate) (PBSA) as the sole carbon source, and could digest PBS and PBSA, as indicated by clearing of the culture supernatant. We purified the PBS-degrading enzyme from the culture supernatant, and its molecular mass was determined as 21.6 kDa. The enzyme was identified as cutinase based on internal amino acid sequences. Specific activities against PBS, PBSA and poly-(lactic acid) (PLA) were determined as 0.42 U/mg, 11 U/mg and 0.067 U/mg, respectively. To obtain a better understanding of how the enzyme recognizes and hydrolyzes PBS/PBSA, we investigated the environment of the catalytic pocket, which is divided into carboxylic acid and alcohol recognition sites. The affinities for different substrates depended on the carbon chain length of the carboxylic acid in the substrate. Competitive inhibition modes were exhibited by carboxylic acids and alcohols that consisted of C4-C6 and C3-C8 chain lengths, respectively. Determination of the affinities for different chemicals indicated that the most preferred substrate for the enzyme would consist of butyric acid and n-hexanol. Title: Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus Nierman WC, Pain A, Anderson MJ, Wortman JR, Kim HS, Arroyo J, Berriman M, Abe K, Archer DB and Denning DW <87 more author(s)> Nierman WC, Pain A, Anderson MJ, Wortman JR, Kim HS, Arroyo J, Berriman M, Abe K, Archer DB, Bermejo C, Bennett J, Bowyer P, Chen D, Collins M, Coulsen R, Davies R, Dyer PS, Farman M, Fedorova N, Feldblyum TV, Fischer R, Fosker N, Fraser A, Garcia JL, Garcia MJ, Goble A, Goldman GH, Gomi K, Griffith-Jones S, Gwilliam R, Haas B, Haas H, Harris D, Horiuchi H, Huang J, Humphray S, Jimenez J, Keller N, Khouri H, Kitamoto K, Kobayashi T, Konzack S, Kulkarni R, Kumagai T, Lafon A, Latge JP, Li W, Lord A, Lu C, Majoros WH, May GS, Miller BL, Mohamoud Y, Molina M, Monod M, Mouyna I, Mulligan S, Murphy L, O'Neil S, Paulsen I, Penalva MA, Pertea M, Price C, Pritchard BL, Quail MA, Rabbinowitsch E, Rawlins N, Rajandream MA, Reichard U, Renauld H, Robson GD, Rodriguez de Cordoba S, Rodriguez-Pena JM, Ronning CM, Rutter S, Salzberg SL, Sanchez M, Sanchez-Ferrero JC, Saunders D, Seeger K, Squares R, Squares S, Takeuchi M, Tekaia F, Turner G, Vazquez de Aldana CR, Weidman J, White O, Woodward J, Yu JH, Fraser C, Galagan JE, Asai K, Machida M, Hall N, Barrell B, Denning DW (- 87) Ref: Nature, 438:1151, 2005 : PubMed ESTHER: Nierman_2005_Nature_438_1151 PubMedSearch: Nierman 2005 Nature 438 1151 PubMedID: 16372009 Gene_locus related to this paper: aspfc-b0xp50, aspfc-b0xu40, aspfc-b0xzj6, aspfc-dpp5, aspfu-apth1, aspfu-axe1, aspfu-CBPYA, aspfu-faec, aspfu-kex1, aspfu-ppme1, aspfu-q4wa39, aspfu-q4wa78, aspfu-q4wf56, aspfu-q4wg73, aspfu-q4wk44, aspfu-q4wkh6, aspfu-q4wnx3, aspfu-q4wpb9, aspfu-q4wqv2, aspfu-q4wub2, aspfu-q4wxr1, aspfu-q4x0n6, aspfu-q4x1n0, aspfu-q5vjg7, neofi-a1cwa6, neofi-a1dfr9, aspfm-a0a084bf80, aspfu-fmac Abstract Aspergillus fumigatus is exceptional among microorganisms in being both a primary and opportunistic pathogen as well as a major allergen. Its conidia production is prolific, and so human respiratory tract exposure is almost constant. A. fumigatus is isolated from human habitats and vegetable compost heaps. In immunocompromised individuals, the incidence of invasive infection can be as high as 50% and the mortality rate is often about 50% (ref. 2). The interaction of A. fumigatus and other airborne fungi with the immune system is increasingly linked to severe asthma and sinusitis. Although the burden of invasive disease caused by A. fumigatus is substantial, the basic biology of the organism is mostly obscure. Here we show the complete 29.4-megabase genome sequence of the clinical isolate Af293, which consists of eight chromosomes containing 9,926 predicted genes. Microarray analysis revealed temperature-dependent expression of distinct sets of genes, as well as 700 A. fumigatus genes not present or significantly diverged in the closely related sexual species Neosartorya fischeri, many of which may have roles in the pathogenicity phenotype. The Af293 genome sequence provides an unparalleled resource for the future understanding of this remarkable fungus. Title: The fungal hydrophobin RolA recruits polyesterase and laterally moves on hydrophobic surfaces Takahashi T, Maeda H, Yoneda S, Ohtaki S, Yamagata Y, Hasegawa F, Gomi K, Nakajima T, Abe K Ref: Molecular Microbiology, 57:1780, 2005 : PubMed ESTHER: Takahashi_2005_Mol.Microbiol_57_1780 PubMedSearch: Takahashi 2005 Mol.Microbiol 57 1780 PubMedID: 16135240 Gene_locus related to this paper: aspor-cutas Abstract When fungi grow on plant or insect surfaces coated with wax polyesters that protect against pathogens, the fungi generally form aerial hyphae to contact the surfaces. Aerial structures such as hyphae and conidiophores are coated with hydrophobins, which are surface-active proteins involved in adhesion to hydrophobic surfaces. When the industrial fungus Aspergillus oryzae was cultivated in a liquid medium containing the biodegradable polyester polybutylene succinate-coadipate (PBSA), the rolA gene encoding hydrophobin RolA was highly transcribed. High levels of RolA and its localization on the cell surface in the presence of PBSA were confirmed by immunostaining. Under these conditions, A. oryzae simultaneously produced the cutinase CutL1, which hydrolyses PBSA. Pre-incubation of PBSA with RolA stimulated PBSA degradation by CutL1, suggesting that RolA bound to the PBSA surface was required for the stimulation. Immunostaining revealed that PBSA films coated with RolA specifically adsorbed CutL1. Quartz crystal microbalance analyses further demonstrated that RolA attached to a hydrophobic sensor chip specifically adsorbed CutL1. Circular dichroism spectra of soluble-state RolA and bound RolA suggested that RolA underwent a conformational change after its adsorption to hydrophobic surfaces. These results suggest that RolA adsorbed to the hydrophobic surface of PBSA recruits CutL1, resulting in condensation of CutL1 on the PBSA surface and consequent stimulation of PBSA hydrolysis. A fluorescence recovery after photobleaching experiment on PBSA films coated with FITC-labelled RolA suggested that RolA moves laterally on the film. We discuss the novel molecular functions of RolA with regard to plastic degradation. Title: Epoxide hydrolase: a mRNA induced by the fungal pathogen Alternaria alternata on rough lemon (Citrus jambhiri Lush) Gomi K, Yamamato H, Akimitsu K Ref: Plant Mol Biol, 53:189, 2003 : PubMed ESTHER: Gomi_2003_Plant.Mol.Biol_53_189 PubMedSearch: Gomi 2003 Plant.Mol.Biol 53 189 PubMedID: 14756316 Gene_locus related to this paper: 9rosi-q76e11 Abstract An expression profile of genes induced by non-pathogenic Alternaria alternata on rough lemon leaves was obtained by sequencing 500 subtractive PCR clones generated from mRNA of leaves inoculated with the fungus after subtraction with that of non-inoculated leaves. About 6% of the cDNA sequences had homology to known putative defense-related genes including epoxide hydrolase. A full-length cDNA (951 bp) from rough lemon that encoded epoxy hydrolase was isolated by random amplification of cDNA ends (RACEs), based on sequence information from subtractive PCR, and designated as RlemEH. The product of this gene expressed with an in vitro translation system with Escherichia coli also had activity of a soluble type of epoxide hydrolase. The transcript of rough lemon RlemEH was not detected in flowers, fruits, stems or leaves, but was induced after inoculation of leaves with conidia of Alternaria alternata, wounding, or treatment with C6 volatiles, including trans-2-hexenol and cis-3-hexenol, and methyl jasmonate. The response of the epoxide hydrolase gene correlated well with the activation of defense mechanisms induced in plant-fungus interactions. | |||||||
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