論文 - 詳細
| RRC ID | 57312 |
|---|---|
| 著者 | Goda S, Koga T, Yamashita K, Kuriura R, Ueda T. |
| タイトル | A novel carbohydrate-binding surface layer protein from the hyperthermophilic archaeon Pyrococcus horikoshii. |
| ジャーナル | Biosci Biotechnol Biochem |
| Abstract |
In Archaea and Bacteria, surface layer (S-layer) proteins form the cell envelope and are involved in cell protection. In the present study, a putative S-layer protein was purified from the crude extract of Pyrococcus horikoshii using affinity chromatography. The S-layer gene was cloned and expressed in Escherichia coli. Isothermal titration calorimetry analyses showed that the S-layer protein bound N-acetylglucosamine and induced agglutination of the gram-positive bacterium Micrococcus lysodeikticus. The protein comprised a 21-mer structure, with a molecular mass of 1,340 kDa, as determined using small-angle X-ray scattering. This protein showed high thermal stability, with a midpoint of thermal denaturation of 79 °C in dynamic light scattering experiments. This is the first description of the carbohydrate-binding archaeal S-layer protein and its characteristics. |
| 巻・号 | 82(8) |
| ページ | 1327-1334 |
| 公開日 | 2018-8-1 |
| DOI | 10.1080/09168451.2018.1460571 |
| PMID | 29629656 |
| MeSH | Acetylglucosamine / metabolism* Amino Acid Sequence Archaeal Proteins / chemistry Archaeal Proteins / genetics Archaeal Proteins / isolation & purification Archaeal Proteins / metabolism* Calorimetry / methods Chromatography, Affinity / methods Cloning, Molecular Electrophoresis, Polyacrylamide Gel Escherichia coli / genetics Genes, Archaeal Green Fluorescent Proteins / metabolism Hot Temperature Micrococcus / metabolism Protein Binding Protein Conformation Protein Denaturation Protein Stability Pyrococcus horikoshii / metabolism* Scattering, Small Angle X-Ray Diffraction |
| IF | 1.297 |
| 引用数 | 0 |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 最多言及媒体 | X(Twitter) |
| 各媒体での言及数の合計 | 1 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| 一般微生物 | JCM 9975 |