Kumagai T

References (13)

Title : Production of recombinant extracellular cholesterol esterase using consistently active promoters in Burkholderia stabilis - Yoshida_2019_Biosci.Biotechnol.Biochem_83_1974
Author(s) : Yoshida K , Konishi K , Magana-Mora A , Rougny A , Yasutake Y , Muramatsu S , Murata S , Kumagai T , Aburatani S , Sakasegawa SI , Tamura T
Ref : Biosci Biotechnol Biochem , 83 :1974 , 2019
Abstract : Burkholderia stabilis FERMP-21014 produces highly active cholesterol esterase in the presence of fatty acids. To develop an overexpression system for cholesterol esterase production, we carried out RNA sequencing analyses to screen strongly active promoters in FERMP-21014. Based on gene expression consistency analysis, we selected nine genes that were consistently expressed at high levels, following which we constructed expression vectors using their promoter sequences and achieved overproduction of extracellular cholesterol esterase under fatty acid-free conditions. Of the tested promoters, the promoter of BSFP_0720, which encodes the alkyl hydroperoxide reductase subunit AhpC, resulted in the highest cholesterol esterase activity (24.3 U mL(-1)). This activity level was 243-fold higher than that of the wild-type strain under fatty acid-free conditions. We confirmed that cholesterol esterase was secreted without excessive accumulation within the cells. The gene expression consistency analysis will be useful to screen promoters applicable to the overexpression of other industrially important enzymes.
ESTHER : Yoshida_2019_Biosci.Biotechnol.Biochem_83_1974
PubMedSearch : Yoshida_2019_Biosci.Biotechnol.Biochem_83_1974
PubMedID: 31216942
Gene_locus related to this paper: 9burk-EstA

Title : Complete Genome Sequence of Burkholderia stabilis FERMP-21014 - Konishi_2017_Genome.Announc_5_
Author(s) : Konishi K , Kumagai T , Sakasegawa SI , Tamura T
Ref : Genome Announc , 5 : , 2017
Abstract : Cholesterol esterase (EC 3.1.1.13) was identified in a bacterium, Burkholderia stabilis strain FERMP-21014. Here, we report the complete genome sequence of B. stabilis FERMP-21014, which has been used in the commercial production of cholesterol esterase. The genome sequence information may be useful for improving production levels of cholesterol esterase.
ESTHER : Konishi_2017_Genome.Announc_5_
PubMedSearch : Konishi_2017_Genome.Announc_5_
PubMedID: 28729264
Gene_locus related to this paper: 9burk-EstA

Title : Identification of a putative FR901469 biosynthesis gene cluster in fungal sp. No. 11243 and enhancement of the productivity by overexpressing the transcription factor gene frbF - Matsui_2017_J.Biosci.Bioeng_123_147
Author(s) : Matsui M , Yokoyama T , Nemoto K , Kumagai T , Terai G , Tamano K , Machida M , Shibata T
Ref : J Biosci Bioeng , 123 :147 , 2017
Abstract : FR901469 is an antifungal antibiotic produced by fungal sp. No. 11243. Here, we searched for FR901469 biosynthesis genes in the genome of No. 11243. Based on the molecular structure of FR901469 and endogenous functional motifs predicted in each genomic NRPS gene, a putative FR901469 biosynthesis gene cluster harboring the most plausible NRPS gene was identified. A transcription factor gene, designated frbF, was found in the cluster. To improve FR901469 productivity, we constructed a strain in which frbF was overexpressed and named it TFH2-2. FR901469 productivity of TFH2-2 was 3.4 times higher than that of the wild-type strain. Transcriptome analysis revealed that most of the genes in the putative FR901469 biosynthesis gene cluster were upregulated in TFH2-2. It also showed that the expression of genes related to ergosterol biosynthesis, beta-1,3-glucan catabolism, and chitin synthesis was inclined to exhibit significant differences in TFH2-2.
ESTHER : Matsui_2017_J.Biosci.Bioeng_123_147
PubMedSearch : Matsui_2017_J.Biosci.Bioeng_123_147
PubMedID: 27660098
Gene_locus related to this paper: blob1-frbd , blob1-frbe

Title : Genome Sequence of Ustilaginoidea virens IPU010, a Rice Pathogenic Fungus Causing False Smut - Kumagai_2016_Genome.Announc_4_e00306
Author(s) : Kumagai T , Ishii T , Terai G , Umemura M , Machida M , Asai K
Ref : Genome Announc , 4 : , 2016
Abstract : Ustilaginoidea virens is a rice pathogenic fungus that causes false smut disease, a disease that seriously damages the yield and quality of the grain. Analysis of the U. virens IPU010 33.6-Mb genome sequence will aid in the understanding of the pathogenicity of the strain, particularly in regard to effector proteins and secondary metabolic genes.
ESTHER : Kumagai_2016_Genome.Announc_4_e00306
PubMedSearch : Kumagai_2016_Genome.Announc_4_e00306
PubMedID: 27151791
Gene_locus related to this paper: 9hypo-a0a063c6x0

Title : Genome Sequence of Fungal Species No.11243, Which Produces the Antifungal Antibiotic FR901469 - Matsui_2015_Genome.Announc_3_e00118
Author(s) : Matsui M , Yokoyama T , Nemoto K , Kumagai T , Terai G , Arita M , Machida M , Shibata T
Ref : Genome Announc , 3 : , 2015
Abstract : Fungal species No.11243 was originally isolated from a decayed leaf sample collected in Kyoto, Japan. It produces FR901469, a 1,3-beta-glucan synthase inhibitor. The genome sequence of No.11243 was determined and annotated to obtain useful information for improving productivity of the effective antifungal agent FR901469.
ESTHER : Matsui_2015_Genome.Announc_3_e00118
PubMedSearch : Matsui_2015_Genome.Announc_3_e00118
PubMedID: 25838475
Gene_locus related to this paper: 9fung-a0a0c9lx98 , 9fung-a0a0c9mdg8 , 9fung-a0a0s6xb63 , 9fung-a0a0s6xf40 , 9fung-a0a0s6xg52 , 9fung-a0a0s6xib3 , 9fung-a0a0s6xiq1 , 9fung-a0a0s6xjc9 , 9fung-a0a0s6xm09 , 9fung-a0a0s6xpa3 , 9fung-a0a0s6xq76 , 9fung-a0a0s6xqa5 , 9fung-a0a0s6xtj4 , 9fung-a0a0s6xvs0 , 9fung-a0a0s6xwu0 , 9fung-a0a0s6xm25 , 9fung-a0a0s6xt75 , blob1-frbd , blob1-frbe

Title : Crystallographic Study To Determine the Substrate Specificity of an L-Serine-Acetylating Enzyme Found in the D-Cycloserine Biosynthetic Pathway - Oda_2013_J.Bacteriol_195_1741
Author(s) : Oda K , Matoba Y , Kumagai T , Noda M , Sugiyama M
Ref : Journal of Bacteriology , 195 :1741 , 2013
Abstract : DcsE, one of the enzymes found in the D-cycloserine biosynthetic pathway, displays a high sequence homology to L-homoserine O-acetyltransferase (HAT), but it prefers L-serine over L-homoserine as the substrate. To clarify the substrate specificity, in the present study we determined the crystal structure of DcsE at a 1.81-angstrom resolution, showing that the overall structure of DcsE is similar to that of HAT, whereas a turn region to form an oxyanion hole is obviously different between DcsE and HAT: in detail, the first and last residues in the turn of DcsE are Gly(52) and Pro(55), respectively, but those of HAT are Ala and Gly, respectively. In addition, more water molecules were laid on one side of the turn region of DcsE than on that of HAT, and a robust hydrogen-bonding network was formed only in DcsE. We created a HAT-like mutant of DcsE in which Gly(52) and Pro(55) were replaced by Ala and Gly, respectively, showing that the mutant acetylates L-homoserine but scarcely acetylates L-serine. The crystal structure of the mutant DcsE shows that the active site, including the turn and its surrounding waters, is similar to that of HAT. These findings suggest that a methyl group of the first residue in the turn of HAT plays a role in excluding the binding of L-serine to the substrate-binding pocket. In contrast, the side chain of the last residue in the turn of DcsE may need to form an extensive hydrogen-bonding network on the turn, which interferes with the binding of L-homoserine.
ESTHER : Oda_2013_J.Bacteriol_195_1741
PubMedSearch : Oda_2013_J.Bacteriol_195_1741
PubMedID: 23396912
Gene_locus related to this paper: strla-d2z028

Title : Crystallographic and mutational analyses of tannase from Lactobacillus plantarum - Matoba_2013_Proteins_81_2052
Author(s) : Matoba Y , Tanaka N , Noda M , Higashikawa F , Kumagai T , Sugiyama M
Ref : Proteins , 81 :2052 , 2013
Abstract : Tannin acylhydrolase (EC 3.1.1.20) referred commonly as tannase catalyzes the hydrolysis of the galloyl ester bond of tannins to release gallic acid. Although the enzyme is useful for various industries, the tertiary structure is not yet determined. In this study, we determined the crystal structure of tannase produced by Lactobacillus plantarum. The tannase structure belongs to a member of alpha/beta-hydrolase superfamily with an additional "lid" domain. A glycerol molecule derived from cryoprotectant solution was accommodated into the tannase active site. The binding manner of glycerol to tannase seems to be similar to that of the galloyl moiety in the substrate. Proteins 2013; 81:2052-2058. (c) 2013 Wiley Periodicals, Inc.
ESTHER : Matoba_2013_Proteins_81_2052
PubMedSearch : Matoba_2013_Proteins_81_2052
PubMedID: 23836494
Gene_locus related to this paper: lacpl-tanL

Title : Structural evidence that puromycin hydrolase is a new type of aminopeptidase with a prolyl oligopeptidase family fold -
Author(s) : Matoba Y , Nakayama A , Oda K , Noda M , Kumagai T , Nishimura M , Sugiyama M
Ref : Proteins , 79 :2999 , 2011
PubMedID: 21905123
Gene_locus related to this paper: strmo-q2hxd9

Title : Molecular cloning and heterologous expression of a biosynthetic gene cluster for the antitubercular agent D-cycloserine produced by Streptomyces lavendulae - Kumagai_2010_Antimicrob.Agents.Chemother_54_1132
Author(s) : Kumagai T , Koyama Y , Oda K , Noda M , Matoba Y , Sugiyama M
Ref : Antimicrobial Agents & Chemotherapy , 54 :1132 , 2010
Abstract : In the present study, we successfully cloned a 21-kb DNA fragment containing a d-cycloserine (DCS) biosynthetic gene cluster from a DCS-producing Streptomyces lavendulae strain, ATCC 11924. The putative gene cluster consists of 10 open reading frames (ORFs), designated dcsA to dcsJ. This cluster includes two ORFs encoding D-alanyl-D-alanine ligase (dcsI) and a putative membrane protein (dcsJ) as the self-resistance determinants of the producer organism, indicated by our previous work. When the 10 ORFs were introduced into DCS-nonproducing Streptomyces lividans 66 as a heterologous host cell, the transformant acquired DCS productivity. This reveals that the introduced genes are responsible for the biosynthesis of DCS. As anticipated, the disruption of dcsG, seen in the DCS biosynthetic gene cluster, made it possible for the strain ATCC 11924 to lose its DCS production. We here propose the DCS biosynthetic pathway. First, L-serine is O acetylated by a dcsE-encoded enzyme homologous to homoserine O-acetyltransferase. Second, O-acetyl-L-serine accepts hydroxyurea via an O-acetylserine sulfhydrylase homolog (dcsD product) and forms O-ureido-L-serine. The hydroxyurea must be supplied by the catalysis of a dcsB-encoded arginase homolog using the L-arginine derivative, N(G)-hydroxy-L-arginine. The resulting O-ureido-L-serine is then racemized to O-ureido-D-serine by a homolog of diaminopimelate epimerase. Finally, O-ureido-D-serine is cyclized to form DCS with the release of ammonia and carbon dioxide. The cyclization must be done by the dcsG or dcsH product, which belongs to the ATP-grasp fold family of protein.
ESTHER : Kumagai_2010_Antimicrob.Agents.Chemother_54_1132
PubMedSearch : Kumagai_2010_Antimicrob.Agents.Chemother_54_1132
PubMedID: 20086163

Title : Genome sequencing and analysis of Aspergillus oryzae - Machida_2005_Nature_438_1157
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
Ref : Nature , 438 :1157 , 2005
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.
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

Title : Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae - Galagan_2005_Nature_438_1105
Author(s) : Galagan JE , Calvo SE , Cuomo C , Ma LJ , Wortman JR , Batzoglou S , Lee SI , Basturkmen M , Spevak CC , Clutterbuck J , Kapitonov V , Jurka J , Scazzocchio C , Farman M , Butler J , Purcell S , Harris S , Braus GH , Draht O , Busch S , d'Enfert C , Bouchier C , Goldman GH , Bell-Pedersen D , Griffiths-Jones S , Doonan JH , Yu J , Vienken K , Pain A , Freitag M , Selker EU , Archer DB , Penalva MA , Oakley BR , Momany M , Tanaka T , Kumagai T , Asai K , Machida M , Nierman WC , Denning DW , Caddick M , Hynes M , Paoletti M , Fischer R , Miller B , Dyer P , Sachs MS , Osmani SA , Birren BW
Ref : Nature , 438 :1105 , 2005
Abstract : The aspergilli comprise a diverse group of filamentous fungi spanning over 200 million years of evolution. Here we report the genome sequence of the model organism Aspergillus nidulans, and a comparative study with Aspergillus fumigatus, a serious human pathogen, and Aspergillus oryzae, used in the production of sake, miso and soy sauce. Our analysis of genome structure provided a quantitative evaluation of forces driving long-term eukaryotic genome evolution. It also led to an experimentally validated model of mating-type locus evolution, suggesting the potential for sexual reproduction in A. fumigatus and A. oryzae. Our analysis of sequence conservation revealed over 5,000 non-coding regions actively conserved across all three species. Within these regions, we identified potential functional elements including a previously uncharacterized TPP riboswitch and motifs suggesting regulation in filamentous fungi by Puf family genes. We further obtained comparative and experimental evidence indicating widespread translational regulation by upstream open reading frames. These results enhance our understanding of these widely studied fungi as well as provide new insight into eukaryotic genome evolution and gene regulation.
ESTHER : Galagan_2005_Nature_438_1105
PubMedSearch : Galagan_2005_Nature_438_1105
PubMedID: 16372000
Gene_locus related to this paper: emeni-axe1 , emeni-BST1 , emeni-c8vrl3 , emeni-CUTI3 , emeni-faec , emeni-ppme1 , emeni-q5aqv0 , emeni-q5ara9 , emeni-q5av79 , emeni-q5avd3 , emeni-q5awc7 , emeni-q5awq3 , emeni-q5awu9 , emeni-q5aww7 , emeni-q5ax50 , emeni-q5ay37 , emeni-q5ay57 , emeni-q5ayk9 , emeni-q5az32 , emeni-q5azl2 , emeni-q5azp1 , emeni-q5b1v2 , emeni-q5b2c1 , emeni-q5b3d2 , emeni-q5b5j7 , emeni-q5b7i6 , emeni-q5b8p6 , emeni-q5b9e7 , emeni-q5b246 , emeni-q5b446 , emeni-q5b602 , emeni-q5b938 , emeni-q5ba78 , emeni-q5bad3 , emeni-q5bar0 , emeni-q5bcd1 , emeni-q5bcd2 , emeni-q5bcf8 , emeni-q5bdr0 , emeni-q5beh9 , emeni-q5bgk7 , emeni-q7si80 , emeni-q5bdv9 , emeni-c8vu15 , 9euro-a0a3d8t644 , emeni-q5b719 , emeni-q5ax97 , emeni-tdia , emeni-afoc , emeni-dbae

Title : Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus - Nierman_2005_Nature_438_1151
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
Ref : Nature , 438 :1151 , 2005
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.
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

Title : Self-protection mechanism in D-cycloserine-producing Streptomyces lavendulae. Gene cloning, characterization, and kinetics of its alanine racemase and D-alanyl-D-alanine ligase, which are target enzymes of D-cycloserine - Noda_2004_J.Biol.Chem_279_46143
Author(s) : Noda M , Kawahara Y , Ichikawa A , Matoba Y , Matsuo H , Lee DG , Kumagai T , Sugiyama M
Ref : Journal of Biological Chemistry , 279 :46143 , 2004
Abstract : An antibiotic, D-cycloserine (DCS), inhibits the catalytic activities of alanine racemase (ALR) and d-alanyl-d-alanine ligase (DDL), which are necessary for the biosynthesis of the bacterial cell wall. In this study, we cloned both genes encoding ALR and DDL, designated alrS and ddlS, respectively, from DCS-producing Streptomyces lavendulae ATCC25233. Each gene product was purified to homogeneity and characterized. Escherichia coli, transformed with a pET vector carrying alrS or ddlS, displays higher resistance to DCS than the same host carrying the E. coli ALR- or DDL-encoded gene inserted into the pET vector. Although the S. lavendulae DDL was competitively inhibited by DCS, the K(i) value (920 microM) was obviously higher (40 approximately 100-fold) than those for E. coli DdlA (9 microM) or DdlB (27 microM). The high K(i) value of the S. lavendulae DDL suggests that the enzyme may be a self-resistance determinant in the DCS-producing microorganism. Kinetic studies for the S. lavendulae ALR suggest that the time-dependent inactivation rate of the enzyme by DCS is absolutely slower than that of the E. coli ALR. We conclude that ALR from DCS-producing S. lavendulae is also one of the self-resistance determinants.
ESTHER : Noda_2004_J.Biol.Chem_279_46143
PubMedSearch : Noda_2004_J.Biol.Chem_279_46143
PubMedID: 15302885
Gene_locus related to this paper: strla-q65yw6