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Putative Alginate Assimilation Process of the Marine Bacterium Saccharophagus degradans 2-40 Based on Quantitative Proteomic Analysis.
Takagi, Toshiyuki; Morisaka, Hironobu; Aburaya, Shunsuke; Tatsukami, Yohei; Kuroda, Kouichi; Ueda, Mitsuyoshi.
Afiliación
  • Takagi T; Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo, Kyoto, 606-8502, Japan. takagi.toshiyuki.42a@st.kyoto-u.ac.jp.
  • Morisaka H; JST, CREST, Kawaguchi, Saitama, 332-0012, Japan. takagi.toshiyuki.42a@st.kyoto-u.ac.jp.
  • Aburaya S; Japan Society for the Promotion of Science, Sakyo, Kyoto, 606-8502, Japan. takagi.toshiyuki.42a@st.kyoto-u.ac.jp.
  • Tatsukami Y; Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo, Kyoto, 606-8502, Japan. morisaka@kais.kyoto-u.ac.jp.
  • Kuroda K; JST, CREST, Kawaguchi, Saitama, 332-0012, Japan. morisaka@kais.kyoto-u.ac.jp.
  • Ueda M; Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo, Kyoto, 606-8502, Japan. aburaya.shunsuke.37r@st.kyoto-u.ac.jp.
Mar Biotechnol (NY) ; 18(1): 15-23, 2016 Feb.
Article en En | MEDLINE | ID: mdl-26458373
Quantitative proteomic analysis was conducted to assess the assimilation processes of Saccharophagus degradans cultured with glucose, pectin, and alginate as carbon sources. A liquid chromatography-tandem mass spectrometry approach was used, employing our unique, long monolithic silica capillary column. In an attempt to select candidate proteins that correlated to alginate assimilation, the production of 23 alginate-specific proteins was identified by statistical analyses of the quantitative proteomic data. Based on the analysis, we propose that S. degradans has an alginate-specific gene cluster for efficient alginate utilization. The alginate-specific proteins of S. degradans were comprised of alginate lyases, enzymes related to carbohydrate metabolism, membrane transporters, and transcription factors. Among them, the short-chain dehydrogenase/reductase Sde_3281 annotated in the alginate-specific cluster showed 4-deoxy-L-erythro-5-hexoseulose uronic acid reductase (DehR) activity. Furthermore, we found two different genes (Sde_3280 and Sde_0939) encoding 2-keto-3-deoxy-D-gluconic acid (KDG) kinases (KdgK) that metabolize the KDG derived from alginate and pectin in S. degradans. S. degradans used Sde_3280 to phosphorylate the KDG derived from alginate and Sde_0939 to phosphorylate the KDG derived from pectin. The distinct selection of KdgKs provides an important clue toward the elucidation of how S. degradans recognizes and processes polysaccharides.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Gammaproteobacteria / Proteoma / Alginatos / Organismos Acuáticos Tipo de estudio: Prognostic_studies Idioma: En Revista: Mar Biotechnol (NY) Asunto de la revista: BIOLOGIA / BIOTECNOLOGIA Año: 2016 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Gammaproteobacteria / Proteoma / Alginatos / Organismos Acuáticos Tipo de estudio: Prognostic_studies Idioma: En Revista: Mar Biotechnol (NY) Asunto de la revista: BIOLOGIA / BIOTECNOLOGIA Año: 2016 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos