Identification of Metabolically Active Bacteria in the Gut of the Generalist <em>Spodoptera littoralis</em> via DNA Stable Isotope Probing Using <sup>13</sup>C-Glucose

Guts of most insects are inhabited by complex communities of symbiotic nonpathogenic bacteria. Within such microbial communities it is possible to ...

Max Planck Institute for Chemical Ecology

To investigate the diversities of Accumulibacter phosphatis and its polyhydroxyalkanoate (PHA) synthase gene (phaC) in enhanced biological phosphorus removal (EBPR) sludge, an acetate-fed sequencing batch reactor was operated. Analysis of microbial communities using fluorescence in situ hybridization and 16S rRNA gene clone libraries showed that the population of Accumulibacter phosphatis in the EBPR sludge comprised more than 50% of total bacteria, and was clearly divided into two subgroups with about 97.5% sequence identity of the 16S rRNA genes. PAO phaC primers targeting the phaC genes of Accumulibacter phosphatis were designed and applied to retrieve fragments of putative phaC homologs of Accumulibacter phosphatis from EBPR sludge. PAO phaC primers targeting G 1PAO, G 2PAO, and G 3PAO groups produced PCR amplicons successfully; the resulting sequences of the phaC gene homologs were diverse, and were distantly related to metagenomic phaC sequences of Accumulibacter phosphatis with 75-98% DNA sequence identities. Degenerate NPAO (non-PAO) phaC primers targeting phaC genes of non- Accumulibacter phosphatis bacteria were also designed and applied to the EBPR sludge. Twenty-four phaC homologs retrieved from NPAO phaC primers were different from the phaC gene homologs derived from Accumulibacter phosphatis, which suggests that the PAO phaC primers were specific for the amplification of phaC gene homologs of Accumulibacter phosphatis, and the putative phaC gene homologs by PAO phaC primers were derived from Accumulibacter phosphatis in the EBPR sludge. Among 24 phaC homologs, a phaC homolog (G1NPAO-2), which was dominant in the NPAO phaC clone library, showed the strongest signal in slot hybridization and shared approximately 60% nucleotide identity with the G4PAO group of Accumulibacter phosphatis, which suggests that G1NPAO-2 might be derived from Accumulibacter phosphatis. In conclusion, analyses of the 16S rRNA and phaC genes showed that Accumulibacter phosphatis might be phylogenetically and metabolically diverse.

Fine-scale population structure of Accumulibacter phosphatis in enhanced biological phosphorus removal sludge.

Two floc-forming, nitrogen-fixing bacteria, strains EMB43(T) and EMB61, obtained from activated sludge of a domestic wastewater treatment plant in Korea, were characterized. The two strains were very closely related, sharing 99.7 % 16S rRNA gene sequence similarity and showing a level of DNA-DNA relatedness of 93 %, which suggests that they represent members of a single species. Phylogenetic analysis based on 16S rRNA gene sequences showed that the two novel isolates formed a distinct phyletic lineage within the genus Zoogloea and were related most closely to Zoogloea resiniphila DhA-35(T) and Zoogloea oryzae A-7(T), with sequence similarities of 97.2 %. Levels of DNA-DNA relatedness between strain EMB43(T) and Z. resiniphila DhA-35(T) and Z. oryzae A-7(T) were 12.8 and 7.4 %, respectively. Cells of strains EMB43(T) and EMB61 were facultatively aerobic, rod-shaped, Gram-negative and motile by means of a polar flagellum. The strains grew at temperatures of 15-40 degrees C (optimum: 25-30 degrees C) and at pH 6.0-9.0 (optimum: pH 6.5-7.5). The predominant fatty acids were C(16 : 0), C(10 : 0) 3-OH and summed feature 3 (C(16 : 1)omega7c and/or iso-C(15 : 0) 2-OH), and the predominant polar lipid was phosphatidylethanolamine. The genomic DNA G+C content was 64.9-65.0 mol% and the major isoprenoid quinone was ubiquinone-8 (Q-8). On the basis of phenotypic, chemotaxonomic and molecular data, the isolates are considered to represent a novel species of the genus Zoogloea, for which the name Zoogloea caeni sp. nov. is proposed. The type strain is EMB43(T) (=KCTC 22084(T)=DSM 19389(T)).

Zoogloea caeni sp. nov., a floc-forming bacterium isolated from activated sludge.

In the animal kingdom, carotenoids are usually absorbed from dietary sources and transported to target tissues. Despite their general importance, the uptake mechanism is still poorly understood. Here we report the "red crop" phenomenon, an accumulation of α- and β-carotene in crystalline inclusions in the enlarged foregut of the polyphagous Spodoptera larvae feeding on some potentially toxic plant leaves. The carotene crystals give the insect foregut a distinctive orange-red color. The crystals are embedded in a homogenous lawn of the bacterium Enterococcus casseliflavus, but the carotene seems to be selectively taken from the food plant. Caterpillars which fail to develop these carotene crystals exhibit a high mortality or fail to develop to adulthood. The crystallization of carotene and the enlargement of the foregut thus appears to manifest a multiple-step physiological adaptation of the insects to toxic food plants.

Crystallization of α- and β-carotene in the foregut of Spodoptera larvae feeding on a toxic food plant.

Sarcosina ossidasi (SOX) catalizza l&#39;ossidazione del gruppo metile in sarcosina e trasferimento del gruppo metile ossidato nel pool metabolico-one in carbonio. Qui, abbiamo separatamente clonato ed espresso subunit&agrave; &alpha; e &beta; di SOX da Thermococcus kodakarensis KOD1 (TkSOX) in Escherichia coli e le proteine ricombinanti sono state purificate di omogeneit&agrave;. Gel filtrazione cromatografia e trasmissione microscopia elettronica analisi ha mostrato che la subunit&agrave; &alpha; formata una struttura dimerica e si comportava come una deidrogenasi NADH; Subunit&agrave; &beta; &egrave; stato un tetramero che aveva Sarcosina ossidasi e l:-attivit&agrave; di prolina deidrogenasi. Il complesso TkSOX assemblati in etero-octameric (&alpha;&beta;)(4) forma e aveva attivit&agrave; di NADH deidrogenasi. Etichetta oro analisi ha indicato che le subunit&agrave; &alpha; e &beta; sono state orientate in forma alternativa. Basato su questi risultati, abbiamo suggerito che TkSOX era un enzima multifunzionale e che ogni subunit&agrave; e (&alpha;&beta;)(4) complesso pu&ograve; esistere separatamente come un enzima funzione in condizioni diverse.

Architettura e caratterizzazione della Sarcosina ossidasi da Thermococcus kodakarensis KOD1.

&#x808C;&#x6C28;&#x9178;&#x6C27;&#x5316;&#x9176; (SOX) &#x50AC;&#x5316;&#x6C27;&#x5316;&#x7532;&#x57FA;&#x7EC4;&#x6C28;&#x9178;&#x5728;&#x548C;&#x6C27;&#x5316;&#x7684;&#x7532;&#x57FA;&#x7EC4;&#x8F6C;&#x5165;&#x4E00;&#x78B3;&#x4EE3;&#x8C22;&#x6C60;&#x3002;&#x5728;&#x8FD9;&#x91CC;&#xFF0C;&#x6211;&#x4EEC;&#x5206;&#x522B;&#x514B;&#x9686;&#x53CA;&#x5728;&#x5927;&#x80A0;&#x6746;&#x83CC;&#x4E2D;&#x8868;&#x8FBE;&#x7684; SOX &#x4ECE; Thermococcus kodakarensis KOD1 (TkSOX) &#x7684; &alpha; &#x548C; &beta; &#x4E9A;&#x57FA;&#x548C;&#x91CD;&#x7EC4;&#x86CB;&#x767D;&#x8D28;&#xFF0C;&#x51C0;&#x5316;&#x7684;&#x540C;&#x8D28;&#x6027;&#x3002;&#x51DD;&#x80F6;&#x8FC7;&#x6EE4;&#x8272;&#x8C31;&#x6CD5;&#x548C;&#x900F;&#x5C04;&#x7535;&#x955C;&#x5206;&#x6790;&#x8868;&#x660E; &alpha; &#x4E9A;&#x57FA;&#x5F62;&#x6210;&#x4E00;&#x4E2A;&#x4E8C;&#x805A;&#x7684;&#x7ED3;&#x6784;&#x548C;&#x8868;&#x73B0;&#x4F5C;&#x4E3A; NADH &#x8131;&#x6C22;&#x9176; &#xFF1B;&Beta; &#x4E9A;&#x57FA;&#x662F;&#x56DB;&#x805A;&#x4F53;&#x808C;&#x6C28;&#x9178;&#x6C27;&#x5316;&#x9176;&#x548C;&#x6BD4;&#x5C14;-&#x812F;&#x6C28;&#x9178;&#x8131;&#x6C22;&#x9176;&#x6D3B;&#x6027;&#x3002;TkSOX &#x590D;&#x6742;&#x7EC4;&#x88C5;&#x6210;&#x5F02;&#x8D28;-octameric (&alpha;&beta;)(4) &#x7A97;&#x4F53;&#x548C;&#x4E86; NADH &#x8131;&#x6C22;&#x9176;&#x6D3B;&#x6027;&#x3002;&#x9EC4;&#x91D1;&#x6807;&#x7B7E;&#x5206;&#x6790;&#x8868;&#x660E; &alpha; &#x548C; &beta; &#x4E9A;&#x57FA;&#x9762;&#x5411;&#x7684;&#x66FF;&#x4EE3;&#x5F62;&#x5F0F;&#x3002;&#x6839;&#x636E;&#x8FD9;&#x4E9B;&#x7ED3;&#x679C;&#xFF0C;&#x6211;&#x4EEC;&#x5EFA;&#x8BAE;&#xFF0C;TkSOX &#x662F;&#x4E00;&#x79CD;&#x591A;&#x529F;&#x80FD;&#x7684;&#x9176;&#xFF0C;&#x6BCF;&#x4E2A;&#x4E9A;&#x57FA; (&alpha;&beta;)(4) &#x590D;&#x6742;&#x5206;&#x5F00;&#x53EF;&#x80FD;&#x5B58;&#x5728;&#x4F5C;&#x4E3A;&#x529F;&#x80FD;&#x9176;&#x5728;&#x4E0D;&#x540C;&#x7684;&#x6761;&#x4EF6;&#x3002;

&#x4F53;&#x7CFB;&#x7ED3;&#x6784;&#x548C; Thermococcus kodakarensis KOD1 &#x808C;&#x6C28;&#x9178;&#x6C27;&#x5316;&#x9176;&#x7684;&#x8868;&#x5F81;&#x3002;

Sarcosine oxidase (SOX) catalyzes the oxidation of the methyl group in sarcosine and transfer of the oxidized methyl group into the one-carbon metabolic pool. Here, we separately cloned and expressed Î± and Î² subunit of SOX from Thermococcus kodakarensis KOD1 (TkSOX) in Escherichia coli and the recombinant proteins were purified to homogeneity. Gel filtration chromatography and transmission electron microscopy analysis showed that the Î± subunit formed a dimeric structure and behaved as an NADH dehydrogenase; Î² subunit was a tetramer that had sarcosine oxidase and L: -proline dehydrogenase activity. The TkSOX complex assembled into the hetero-octameric (Î±Î²)(4) form and had NADH dehydrogenase activity. Gold-label analysis indicated that Î± and Î² subunits were oriented in the alternative form. Based on these results, we suggested that TkSOX was a multifunctional enzyme and that each subunit and (Î±Î²)(4) complex may separately exist as a function enzyme in different conditions.

Architecture and characterization of sarcosine oxidase from Thermococcus kodakarensis KOD1.

Sarcosine oxydase (SOX) catalyse l&#39;oxydation du groupe m&eacute;thyle dans la sarcosine et le transfert du groupe m&eacute;thyle oxyd&eacute; dans le pool m&eacute;tabolique d&#39;un carbone. Ici, nous s&eacute;par&eacute;ment clon&eacute; et exprim&eacute; des sous-unit&eacute;s &alpha; et &beta; de SOX de Thermococcus kodakarensis KOD1 (TkSOX) chez Escherichia coli et les prot&eacute;ines recombinantes ont &eacute;t&eacute; purifi&eacute;es jusqu&#39;&agrave; homog&eacute;n&eacute;it&eacute;. Gel filtration chromatographie et transmission electron microscopy analyse a montr&eacute; que la sous-unit&eacute; &alpha; form&eacute; d&#39;une structure de dim&egrave;re et s&#39;est comport&eacute; comme une NADH d&eacute;shydrog&eacute;nase ; Sous-unit&eacute; de &beta; est un t&eacute;tram&egrave;re qui avait la sarcosine oxydase et L:-activit&eacute; proline d&eacute;shydrog&eacute;nase. Le complexe TkSOX assembl&eacute;s dans l&#39;h&eacute;t&eacute;ro-et (formulaire &alpha;&beta;)(4) et avait une activit&eacute; NADH d&eacute;shydrog&eacute;nase. Or-&eacute;tiquette analyse a indiqu&eacute; que les sous-unit&eacute;s &alpha; et &beta; sont construites sous la forme alternative. Selon ces r&eacute;sultats, nous avons sugg&eacute;r&eacute; que TkSOX &eacute;tait une enzyme multifonctionnelle et que chacune des sous-unit&eacute;s et (complexe &alpha;&beta;)(4) peut il existe s&eacute;par&eacute;ment comme une enzyme en fonction dans des conditions diff&eacute;rentes.

Architecture et caract&eacute;risation de la sarcosine oxydase de Thermococcus kodakarensis KOD1.

Sarkosin Oxydase (SOX) katalysiert die Oxidation der Methylgruppe in Sarkosin und Transfer der oxidierten Methyl-Gruppe in den Stoffwechsel ein-Kohlenstoff-Pool. Hier wir separat kloniert und &alpha; und &beta;-Untereinheit des SOX aus Thermococcus Kodakarensis KOD1 (TkSOX) in Escherichia coli ausgedr&uuml;ckt und die rekombinante Proteine zur Homogenit&auml;t gereinigt wurden. Gel Filtration Chromatographie und &Uuml;bertragung Elektronenmikroskopie Analyse zeigte, dass die &alpha;-Untereinheit eine Dimere Struktur bildeten und eine NADH-Dehydrogenase Verhalten; &Beta;-Untereinheit war ein Tetramer, das Sarkosin Oxydase und L: hatte-Prolin Dehydrogenase-Aktivit&auml;t. Die TkSOX-Anlage montiert in der Hetero-Octameric (&alpha;&beta;)(4) Form und hatte NADH-Dehydrogenase-Aktivit&auml;t. Gold-Etikett-Untersuchung ergab, dass &alpha; und &beta;-Untereinheiten in alternativer Form orientiert waren. Auf der Grundlage dieser Ergebnisse wir vorgeschlagen, dass TkSOX ein multifunktionelles Enzym und sei jeder Untereinheit und (&alpha;&beta;)(4)-Komplex kann separat existieren als ein Enzym Funktion unter verschiedenen Bedingungen.

Architektur und Charakterisierung von Sarkosin Oxydase aus Thermococcus Kodakarensis KOD1.

&#x30B5;&#x30EB;&#x30B3;&#x30B7;&#x30F3;&#x9178;&#x5316;&#x9175;&#x7D20; (SOX) &#x30B5;&#x30EB;&#x30B3;&#x30B7;&#x30F3;&#x306E;&#x30E1;&#x30C1;&#x30EB;&#x57FA;&#x306E;&#x9178;&#x5316;&#x3068;&#x9178;&#x5316;&#x30E1;&#x30C1;&#x30EB; &#x30B0;&#x30EB;&#x30FC;&#x30D7;&#x306E;&#x8EE2;&#x9001; 1 &#x70AD;&#x7D20;&#x4EE3;&#x8B1D;&#x30D7;&#x30FC;&#x30EB;&#x306B;&#x89E6;&#x5A92;&#x4F5C;&#x7528;&#x3092;&#x53CA;&#x307C;&#x3057;&#x307E;&#x3059;&#x3002;&#x3053;&#x3053;&#x3067;&#x306F;&#x3001;&#x5225;&#x3005; &#x306B;&#x8907;&#x88FD;&#x3057;&#x3001;&alpha; &#x3068; &beta; &#x30B5;&#x30D6;&#x30E6;&#x30CB;&#x30C3;&#x30C8; &#x30BD;&#x30C3;&#x30AF;&#x30B9; (TkSOX) &#x30B5;&#x30FC;&#x30E2;&#x30B3;&#x30C3;&#x30AB;&#x30B9;&#x5C5E; kodakarensis KOD1 &#x304B;&#x3089;&#x306E;&#x5927;&#x8178;&#x83CC;&#x3067;&#x306E;&#x767A;&#x73FE;&#x3057;&#x3001;&#x7D44;&#x63DB;&#x3048;&#x30BF;&#x30F3;&#x30D1;&#x30AF;&#x8CEA;&#x540C;&#x8CEA;&#x6027;&#x306B;&#x6D44;&#x5316;&#x3055;&#x308C;&#x307E;&#x3057;&#x305F;&#x3002;&#x30B2;&#x30EB;&#x6FFE;&#x904E;&#x30AF;&#x30ED;&#x30DE;&#x30C8;&#x30B0;&#x30E9;&#x30D5;&#x30A3;&#x30FC;&#x3068;&#x900F;&#x904E;&#x96FB;&#x5B50;&#x9855;&#x5FAE;&#x93E1;&#x306B;&#x3088;&#x308B;&#x89E3;&#x6790;&#x306F;&#x3001;&alpha; &#x30B5;&#x30D6;&#x30E6;&#x30CB;&#x30C3;&#x30C8;&#x306F;&#x4E8C;&#x91CF;&#x4F53;&#x69CB;&#x9020;&#x3092;&#x5F62;&#x6210;&#x3057;&#x3001;NADH &#x8131;&#x6C34;&#x7D20;&#x9175;&#x7D20;&#x3068;&#x3057;&#x3066;&#x306E;&#x884C;&#x5100;&#x3092;&#x793A;&#x3057;&#x305F;;&Beta; &#x30B5;&#x30D6;&#x30E6;&#x30CB;&#x30C3;&#x30C8;&#x3060;&#x3063;&#x305F;&#x30B5;&#x30EB;&#x30B3;&#x30B7;&#x30F3;&#x30AA;&#x30AD;&#x30B7;&#x30C0;&#x30FC;&#x30BC;&#x3068; l: &#x3044;&#x305F;&#x30C6;&#x30C8;&#x30E9;&#x30DE;&#x30FC;-&#x30D7;&#x30ED;&#x30EA;&#x30F3;&#x8131;&#x6C34;&#x7D20;&#x9175;&#x7D20;&#x6D3B;&#x6027;&#x3002;TkSOX &#x8907;&#x96D1;&#x306A;&#x7D44;&#x307F;&#x7ACB;&#x3066;&#x306B;&#x30D8;&#x30C6;&#x30ED; octameric &#xFF08;&alpha;&beta;)(4) &#x30D5;&#x30A9;&#x30FC;&#x30E0;&#x3068; NADH &#x8131;&#x6C34;&#x7D20;&#x9175;&#x7D20;&#x6D3B;&#x6027;&#x304C;&#x3042;&#x3063;&#x305F;&#x3002;&#x30B4;&#x30FC;&#x30EB;&#x30C9; &#x30E9;&#x30D9;&#x30EB;&#x5206;&#x6790; &alpha; &#x3068; &beta; &#x30B5;&#x30D6;&#x30E6;&#x30CB;&#x30C3;&#x30C8;&#x306E;&#x5225;&#x306E;&#x30D5;&#x30A9;&#x30FC;&#x30E0;&#x3067;&#x6307;&#x5411;&#x3055;&#x308C;&#x305F;&#x3053;&#x3068;&#x304C;&#x793A;&#x3055;&#x308C;&#x307E;&#x3057;&#x305F;&#x3002;&#x3053;&#x308C;&#x3089;&#x306E;&#x7D50;&#x679C;&#x306B;&#x57FA;&#x3065;&#x3044;&#x3066;&#x3001;&#x6211;&#x3005; TkSOX &#x591A;&#x6A5F;&#x80FD;&#x9175;&#x7D20;&#x3068;&#x305D;&#x306E;&#x3053;&#x3068;&#x304C;&#x793A;&#x5506;&#x3055;&#x308C;&#x305F;&#x5404;&#x30B5;&#x30D6;&#x30E6;&#x30CB;&#x30C3;&#x30C8;&#x3068; &#xFF08;&alpha;&beta;)(4) &#x30B3;&#x30F3;&#x30D7;&#x30EC;&#x30C3;&#x30AF;&#x30B9;&#x304C;&#x3042;&#x308A;&#x307E;&#x3059;&#x5225;&#x3005; &#x3068;&#x3057;&#x3066;&#x5B58;&#x5728;&#x3059;&#x308B;&#x6A5F;&#x80FD;&#x9175;&#x7D20;&#x306E;&#x7570;&#x306A;&#x308B;&#x6761;&#x4EF6;&#x3067;&#x3002;

&#x30A2;&#x30FC;&#x30AD;&#x30C6;&#x30AF;&#x30C1;&#x30E3;&#x3068;&#x30B5;&#x30EB;&#x30B3;&#x30B7;&#x30F3; &#x30AA;&#x30AD;&#x30B7;&#x30C0;&#x30FC;&#x30BC; &#x30B5;&#x30FC;&#x30E2;&#x30B3;&#x30C3;&#x30AB;&#x30B9;&#x5C5E; kodakarensis KOD1 &#x304B;&#x3089;&#x3002;

Sarcosine &#xC0B0;&#xD654; &#xD6A8;&#xC18C; (SOX) catalyzes sarcosine&#xC5D0; &#xBA54; &#xD2F8; &#xADF8;&#xB8F9; &#xC0B0;&#xD654; &#xBC0F; &#xC0B0;&#xD654; &#xBA54; &#xD2F8; &#xADF8;&#xB8F9;&#xC758; &#xD55C; &#xD0C4;&#xC18C; &#xB300;&#xC0AC; &#xD480;&#xC73C;&#xB85C; &#xC804;&#xC1A1; &#xD569;&#xB2C8;&#xB2E4;. &#xC5EC;&#xAE30;, &#xC6B0;&#xB9AC;&#xAC00; &#xAC1C;&#xBCC4;&#xC801;&#xC73C;&#xB85C; &#xBCF5;&#xC81C; &#xD558; &#xACE0; &#xB300;&#xC7A5;&#xADE0;&#xC5D0; &#xC0AD;&#xC2A4;&#xC5D0;&#xC11C; Thermococcus kodakarensis KOD1 (TkSOX)&#xC758; &alpha;&#xC640; &beta; &#xC18C; &#xB2E8;&#xC704;&#xB97C; &#xD45C;&#xD604; &#xD558; &#xACE0; &#xC7AC;&#xC870;&#xD569; &#xB2E8;&#xBC31;&#xC9C8; &#xB3D9;&#xC9C8;&#xC131;&#xC744; &#xC815;&#xD654; &#xD588;&#xB2E4;. &#xC824; &#xC5EC;&#xACFC; &#xCC29; &#xC0C9; &#xC778;&#xC1C4;&#xAE30; &#xBC0F; &#xC804;&#xC1A1; &#xC804;&#xC790; &#xD604;&#xBBF8;&#xACBD; &#xBD84;&#xC11D;&#xC774; &#xBCF4;&#xC600;&#xB2E4; &alpha; &#xC18C; &#xB2E8;&#xC704; dimeric &#xAD6C;&#xC870;&#xB97C; &#xD615;&#xC131; &#xD558; &#xACE0; &#xD589;&#xB3D9;&#xC73C;&#xB85C; NADH &#xD6A8;&#xC18C;; &Beta; &#xC18C; &#xB2E8;&#xC704;&#xB294; sarcosine &#xC0B0;&#xD654; &#xD6A8;&#xC18C;&#xAC00; &#xC84C;&#xACE0; l: tetramer-&#xD504;&#xB864;&#xB9B0; &#xD6A8;&#xC18C; &#xD65C;&#xB3D9;. Hetero-octameric&#xC5D0; TkSOX &#xBCF5;&#xC7A1; &#xD55C; &#xC870;&#xB9BD; (&alpha;&beta;)(4) &#xC591;&#xC2DD; NADH &#xD6A8;&#xC18C; &#xD65C;&#xB3D9;&#xC744; &#xD588;&#xB2E4;. &#xACE8;&#xB4DC; &#xB77C;&#xBCA8; &#xBD84;&#xC11D; &#xD45C;&#xC2DC; &alpha;&#xC640; &beta; &#xC18C; &#xB2E8;&#xC704; &#xB300;&#xCCB4; &#xD615;&#xD0DC;&#xB85C; &#xC9C0;&#xD5A5; &#xD588;&#xB2E4;. &#xC6B0;&#xB9AC; Tksox&#xB294; &#xB2E4;&#xAE30;&#xB2A5; &#xD6A8;&#xC18C; &#xBC0F; &#xADF8; &#xC81C;&#xC548; &#xC774;&#xB7EC;&#xD55C; &#xACB0;&#xACFC; &#xBC14;&#xD0D5;&#xC73C;&#xB85C;, &#xAC01; &#xC18C; &#xB2E8;&#xC704; (&alpha;&beta;)(4) &#xBCF5;&#xD569; &#xBCC4;&#xB3C4;&#xB85C; &#xB2E4;&#xB978; &#xC870;&#xAC74;&#xC5D0;&#xC11C; &#xD568;&#xC218; &#xD6A8;&#xC18C;&#xB85C; &#xC874;&#xC7AC;&#xD560; &#xC218; &#xC788;&#xC2B5;&#xB2C8;&#xB2E4;.

&#xAC74;&#xCD95;&#xACFC;&#xC5D0;&#xC11C; Thermococcus kodakarensis KOD1 sarcosine &#xC0B0;&#xD654; &#xD6A8;&#xC18C;&#xC758; &#xD2B9;&#xC131; &#xBD84;&#xC11D;.

Sarcosina oxidasa (SOX) cataliza la oxidaci&oacute;n del grupo metilo en sarcosina y transferencia del grupo metilo oxidado en la piscina metab&oacute;lica-carbono. Aqu&iacute;, nosotros por separado hab&iacute;a clonado y hab&iacute;a expresado la subunidad &alpha; y &beta; de SOX de Thermococcus kodakarensis KOD1 (TkSOX) en Escherichia coli y las prote&iacute;nas recombinantes se purificaron a homogeneidad. Gel filtraci&oacute;n cromatograf&iacute;a y transmisi&oacute;n microscopia electr&oacute;nica an&aacute;lisis demostr&oacute; que la subunidad &alpha; formado una estructura dim&eacute;rica y se comport&oacute; como una NADH deshidrogenasa; La subunidad &beta; fue un tetr&aacute;mero que ten&iacute;a sarcosina oxidasa y L:-actividad de la deshidrogenasa de prolina. El complejo de TkSOX montado en el hetero-oct&aacute;merico (forma &alpha;&beta;)(4) y ten&iacute;a la actividad de la NADH deshidrogenasa. Etiqueta oro an&aacute;lisis indic&oacute; que las subunidades &alpha; y &beta; fueron orientadas en forma alternativa. Basado en estos resultados, sugerimos que TkSOX es una enzima multifuncional y que cada subunidad y (complejo &alpha;&beta;)(4) puede existir por separado como una enzima de la funci&oacute;n en diferentes condiciones.

Arquitectura y caracterizaci&oacute;n de sarcosina-oxidasa de Thermococcus kodakarensis KOD1.

The gut of most insects harbours nonpathogenic microorganisms. Recent work suggests that gut microbiota not only provide nutrients, but also involve in the development and maintenance of the host immune system. However, the complexity, dynamics and types of interactions between the insect hosts and their gut microbiota are far from being well understood.

Yongqi Shao

Department of Bioorganic Chemistry

Max Planck Institute for Chemical Ecology

Identification of Metabolically Active Bacteria in the Gut of the Generalist Spodoptera littoralis via DNA Stable Isotope Probing Using ¹³C-Glucose

Yongqi Shao

.css-o250i3{font-size:18px;font-family:Open Sans,sans-serif;line-height:21.6px;}Department of Bioorganic Chemistry

Max Planck Institute for Chemical Ecology

Identification of Metabolically Active Bacteria in the Gut of the Generalist Spodoptera littoralis via DNA Stable Isotope Probing Using 13C-Glucose

Department of Bioorganic Chemistry

Identification of Metabolically Active Bacteria in the Gut of the Generalist Spodoptera littoralis via DNA Stable Isotope Probing Using ¹³C-Glucose