Matsuo Y

References (7)

Title : Novel splice site mutation in LIPH identified in a Japanese patient with autosomal recessive woolly hair -
Author(s) : Matsuo Y , Tanaka A , Shimomura Y , Hide M
Ref : J Dermatol , 43 :1384 , 2016
PubMedID: 27094727
Gene_locus related to this paper: human-LIPH

Title : Ilumatobacter nonamiense sp. nov. and Ilumatobacter coccineum sp. nov., isolated from seashore sand - Matsumoto_2013_Int.J.Syst.Evol.Microbiol_63_3404
Author(s) : Matsumoto A , Kasai H , Matsuo Y , Shizuri Y , Ichikawa N , Fujita N , Omura S , Takahashi Y
Ref : Int J Syst Evol Microbiol , 63 :3404 , 2013
Abstract : Bacterial strains YM16-303(T) and YM16-304(T) were isolated from a sample of seashore sand using a medium with an artificial seawater base. Both isolates grew slowly on marine agar, and were found to be Gram-reaction-positive, aerobic, non-motile and rod-shaped. The cell-wall peptidoglycan contained ll-diaminopimelic acid, glycine, alanine and hydroxyglutamic acid, and the acyl type of the muramic acid was glycolyl. The predominant menaquinone was MK-9(H8). The 16S rRNA gene sequences of strains YM16-303(T) and YM16-304(T) were most similar to that of Ilumatobacter fluminis YM22-133(T), and phylogenetic analyses also indicated that they belong to the genus Ilumatobacter. Ilumatobacter fluminis YM22-133(T) and strains YM16-303(T) and YM16-304(T) should be classified as distinct species in the genus Ilumatobacter, however, since the 16S rRNA gene sequence similarity between them was low and the major cellular fatty acids and some physiological properties were different. Moreover, average nucleotide identity and maximal unique exact matches index values also supported the conclusion that they represent different species. On the basis of the above analyses, two novel species, Ilumatobacter nonamiense sp. nov. (type strain YM16-303(T) = NBRC 109120(T) = KCTC 29139(T)) and Ilumatobacter coccineum sp. nov. (type strain YM16-304(T) = NBRC 103263(T) = KCTC 29153(T)), are proposed. The order Acidimicrobiales, which contains the genus Ilumatobacter, currently includes six genera and only six species, and they are phylogenetically very far from each other. Phylogenetic analyses revealed that strains YM16-303(T) and YM16-304(T) clustered with closely related uncultured actinobacteria but not Ilumatobacter fluminis YM22-133(T), suggesting that many uncultured bacteria related to these isolates exist in the environment. This is the first report on interspecies relationships in the order Acidimicrobiales.
ESTHER : Matsumoto_2013_Int.J.Syst.Evol.Microbiol_63_3404
PubMedSearch : Matsumoto_2013_Int.J.Syst.Evol.Microbiol_63_3404
PubMedID: 23524358
Gene_locus related to this paper: 9actn-m5a1u1 , 9actn-m5ata2 , 9actn-m5a3u3 , 9actn-m5a4d8

Title : Complete genome sequence of the soil actinomycete Kocuria rhizophila - Takarada_2008_J.Bacteriol_190_4139
Author(s) : Takarada H , Sekine M , Kosugi H , Matsuo Y , Fujisawa T , Omata S , Kishi E , Shimizu A , Tsukatani N , Tanikawa S , Fujita N , Harayama S
Ref : Journal of Bacteriology , 190 :4139 , 2008
Abstract : The soil actinomycete Kocuria rhizophila belongs to the suborder Micrococcineae, a divergent bacterial group for which only a limited amount of genomic information is currently available. K. rhizophila is also important in industrial applications; e.g., it is commonly used as a standard quality control strain for antimicrobial susceptibility testing. Sequencing and annotation of the genome of K. rhizophila DC2201 (NBRC 103217) revealed a single circular chromosome (2,697,540 bp; G+C content of 71.16%) containing 2,357 predicted protein-coding genes. Most of the predicted proteins (87.7%) were orthologous to actinobacterial proteins, and the genome showed fairly good conservation of synteny with taxonomically related actinobacterial genomes. On the other hand, the genome seems to encode much smaller numbers of proteins necessary for secondary metabolism (one each of nonribosomal peptide synthetase and type III polyketide synthase), transcriptional regulation, and lateral gene transfer, reflecting the small genome size. The presence of probable metabolic pathways for the transformation of phenolic compounds generated from the decomposition of plant materials, and the presence of a large number of genes associated with membrane transport, particularly amino acid transporters and drug efflux pumps, may contribute to the organism's utilization of root exudates, as well as the tolerance to various organic compounds.
ESTHER : Takarada_2008_J.Bacteriol_190_4139
PubMedSearch : Takarada_2008_J.Bacteriol_190_4139
PubMedID: 18408034
Gene_locus related to this paper: kocrd-b2ggb9 , kocrd-b2gh24 , kocrd-b2ghy5 , kocrd-b2gi73 , kocrd-b2gih2 , kocrd-b2gix1 , kocrd-b2gjc9 , kocrd-b2gk02 , kocrd-b2gk84 , kocrd-b2gkb8 , kocrd-b2gl03

Title : Sequence analysis of three plasmids harboured in Rhodococcus erythropolis strain PR4 - Sekine_2006_Environ.Microbiol_8_334
Author(s) : Sekine M , Tanikawa S , Omata S , Saito M , Fujisawa T , Tsukatani N , Tajima T , Sekigawa T , Kosugi H , Matsuo Y , Nishiko R , Imamura K , Ito M , Narita H , Tago S , Fujita N , Harayama S
Ref : Environ Microbiol , 8 :334 , 2006
Abstract : Rhodococcus erythropolis strain PR4 has been isolated as an alkane-degrading bacterium. The strain harbours one linear plasmid, pREL1 (271 577 bp) and two circular plasmids, pREC1 (104 014 bp) and pREC2 (3637 bp), all with some sequence similarities to other Rhodococcus plasmids. For pREL1, pREC1 and pREC2, 298, 102 and 3 open reading frames, respectively, were predicted. Linear plasmid pREL1 has several regions homologous to plasmid pBD2 found in R. erythropolis BD2. Sequence analysis of pREL1 and pBD2 identified common metal-resistance genes on both, but pREL1 also encodes alkane-degradation genes not found on pBD2, with enzyme constituents some of which are quite different from those of other organisms. The alkane hydroxylase consisted of a cytochrome P450 monooxygenase, a 2Fe-2S ferredoxin, and a ferredoxin reductase. The ferredoxin reductase amino acid sequence resembles the AlkT (rubredoxin reductase) sequence. A zinc-containing alcohol dehydrogenase further oxydizes alkanols, alkane oxidation products catalysed by alkane hydroxylase. Of the circular plasmids, the pREC1 sequence is partially similar to the sequence of pREAT701, the virulence plasmid found in Rhodococcus equi. pREC1 has no pREAT701 virulence genes and encodes genes for beta-oxidation of fatty acids. Thus, joint actions of enzymes encoded by pREL1 and pREC1 may enable efficient mineralization of alkanes.
ESTHER : Sekine_2006_Environ.Microbiol_8_334
PubMedSearch : Sekine_2006_Environ.Microbiol_8_334
PubMedID: 16423019
Gene_locus related to this paper: rhosp-AHY95170 , rhoe4-c0zm41 , rhoe4-c0zny8 , rhoe4-c0zp51 , rhoe4-c0zp80 , rhoe4-c0zpm5 , rhoe4-c0zq56 , rhoe4-c0zq93 , rhoe4-c0zri5 , rhoe4-c0zse4 , rhoe4-c0ztk5 , rhoe4-c0ztv6 , rhoe4-c0ztz5 , rhoe4-c0zw14 , rhoe4-c0zyp1 , rhoe4-c1a1s7 , rhoe4-c1a149 , rhoe4-c1a168 , rhoe4-q3l9i4 , rhoe4-q3l9v3 , rhoe4-q3l9y4 , rhoe4-q3l922 , rhoe4-q3la05 , rhoer-c3jd87 , rhoer-c3jdh1 , rhoer-c3jfg3 , rhoer-c3jfu1 , rhoer-c3jfv6 , rhoer-c3jfw7 , rhoer-c3jg26 , rhoer-c3jgc0 , rhoer-c3jgr8 , rhoer-c3ji24 , rhoer-c3jif3 , rhoer-c3jif5 , rhoer-c3jif6 , rhoer-c3jiw5 , rhoer-c3jl72 , rhoer-c3jle6 , rhoer-c3jmu4 , rhoer-c3jqd8 , rhoer-c3jqd9 , rhoer-c3jqg3 , rhoer-c3jqn9 , rhoer-c3jqs1 , rhoer-c3jr01 , rhoer-c3jrb8 , rhoer-c3jt01 , rhoer-c3jtx3 , rhoer-c3jtx4 , rhoer-c3jvx6 , rhoer-c3jwe1 , rhoer-c3jwn8 , rhosp-bphD2 , rhoe4-c0zua7

Title : Functional annotation of a full-length mouse cDNA collection - Kawai_2001_Nature_409_685
Author(s) : Kawai J , Shinagawa A , Shibata K , Yoshino M , Itoh M , Ishii Y , Arakawa T , Hara A , Fukunishi Y , Konno H , Adachi J , Fukuda S , Aizawa K , Izawa M , Nishi K , Kiyosawa H , Kondo S , Yamanaka I , Saito T , Okazaki Y , Gojobori T , Bono H , Kasukawa T , Saito R , Kadota K , Matsuda H , Ashburner M , Batalov S , Casavant T , Fleischmann W , Gaasterland T , Gissi C , King B , Kochiwa H , Kuehl P , Lewis S , Matsuo Y , Nikaido I , Pesole G , Quackenbush J , Schriml LM , Staubli F , Suzuki R , Tomita M , Wagner L , Washio T , Sakai K , Okido T , Furuno M , Aono H , Baldarelli R , Barsh G , Blake J , Boffelli D , Bojunga N , Carninci P , de Bonaldo MF , Brownstein MJ , Bult C , Fletcher C , Fujita M , Gariboldi M , Gustincich S , Hill D , Hofmann M , Hume DA , Kamiya M , Lee NH , Lyons P , Marchionni L , Mashima J , Mazzarelli J , Mombaerts P , Nordone P , Ring B , Ringwald M , Rodriguez I , Sakamoto N , Sasaki H , Sato K , Schonbach C , Seya T , Shibata Y , Storch KF , Suzuki H , Toyo-oka K , Wang KH , Weitz C , Whittaker C , Wilming L , Wynshaw-Boris A , Yoshida K , Hasegawa Y , Kawaji H , Kohtsuki S , Hayashizaki Y
Ref : Nature , 409 :685 , 2001
Abstract : The RIKEN Mouse Gene Encyclopaedia Project, a systematic approach to determining the full coding potential of the mouse genome, involves collection and sequencing of full-length complementary DNAs and physical mapping of the corresponding genes to the mouse genome. We organized an international functional annotation meeting (FANTOM) to annotate the first 21,076 cDNAs to be analysed in this project. Here we describe the first RIKEN clone collection, which is one of the largest described for any organism. Analysis of these cDNAs extends known gene families and identifies new ones.
ESTHER : Kawai_2001_Nature_409_685
PubMedSearch : Kawai_2001_Nature_409_685
PubMedID: 11217851
Gene_locus related to this paper: mouse-1lipg , mouse-1plip , mouse-1plrp , mouse-ABH15 , mouse-abhd5 , mouse-ABHD6 , mouse-Abhd8 , mouse-aryla , mouse-bphl , mouse-cauxin , mouse-Ces1g , mouse-CPMac , mouse-dpp8 , mouse-EPHX1 , mouse-ES10 , mouse-hslip , mouse-hyes , mouse-ABHD2 , mouse-lcat , mouse-lipli , mouse-LIPN , mouse-lypla1 , mouse-lypla2 , mouse-OVCA2 , mouse-pafa , mouse-pcp , mouse-Ppgb , mouse-PPME1 , mouse-ppt , mouse-q3uuq7 , mouse-Q9DAI6 , mouse-Q80UX8 , mouse-RISC , mouse-SERHL , mouse-SPG21 , mouse-Tex30

Title : Identification of catalytically essential residues in Escherichia coli esterase by site-directed mutagenesis - Haruki_1999_FEBS.Lett_454_262
Author(s) : Haruki M , Oohashi Y , Mizuguchi S , Matsuo Y , Morikawa M , Kanaya S
Ref : FEBS Letters , 454 :262 , 1999
Abstract : Escherichia coli esterase (EcE) is a member of the hormone-sensitive lipase family. We have analyzed the roles of the conserved residues in this enzyme (His103, Glu128, Gly163, Asp164, Ser165, Gly167, Asp262, Asp266 and His292) by site-directed mutagenesis. Among them, Gly163, Asp164, Ser165, and Gly167 are the components of a G-D/E-S-A-G motif. We showed that Ser165, Asp262, and His292 are the active-site residues of the enzyme. We also showed that none of the other residues, except for Asp164, is critical for the enzymatic activity. The mutation of Asp164 to Ala dramatically reduced the catalytic efficiency of the enzyme by the factor of 10(4) without seriously affecting the substrate binding. This residue is probably structurally important to make the conformation of the active-site functional.
ESTHER : Haruki_1999_FEBS.Lett_454_262
PubMedSearch : Haruki_1999_FEBS.Lett_454_262
PubMedID: 10431819
Gene_locus related to this paper: ecoli-Aes

Title : Measurement of lipase activity of guinea pig peritoneal macrophages with 4-methylumbelliferyl-oleate -
Author(s) : Kiyotani K , Tasaka H , Matsuo Y
Ref : Hiroshima J Med Sci , 32 :15 , 1983
PubMedID: 6688069