論文 - 詳細
| RRC ID | 39658 |
|---|---|
| 著者 | Watanabe-Nakayama T, Itami M, Kodera N, Ando T, Konno H. |
| タイトル | High-speed atomic force microscopy reveals strongly polarized movement of clostridial collagenase along collagen fibrils. |
| ジャーナル | Sci Rep |
| Abstract |
Bacterial collagenases involved in donor infection are widely applied in many fields due to their high activity and specificity; however, little is known regarding the mechanisms by which bacterial collagenases degrade insoluble collagen in host tissues. Using high-speed atomic force microscopy, we simultaneously visualized the hierarchical structure of collagen fibrils and the movement of a representative bacterial collagenase, Clostridium histolyticum type I collagenase (ColG), to determine the relationship between collagen structure and collagenase movement. Notably, ColG moved ~14.5 nm toward the collagen N terminus in ~3.8 s in a manner dependent on a catalytic zinc ion. While ColG was engaged, collagen molecules were not only degraded but also occasionally rearranged to thicken neighboring collagen fibrils. Importantly, we found a similarity of relationship between the enzyme-substrate interface structure and enzyme migration in collagen-collagenase and DNA-nuclease systems, which share a helical substrate structure, suggesting a common strategy in enzyme evolution. |
| 巻・号 | 6 |
| ページ | 28975 |
| 公開日 | 2016-7-4 |
| DOI | 10.1038/srep28975 |
| PII | srep28975 |
| PMID | 27373458 |
| PMC | PMC4931465 |
| MeSH | Clostridium histolyticum / enzymology* Coenzymes / metabolism Collagen / metabolism* Microbial Collagenase / metabolism* Microscopy, Atomic Force Proteolysis Zinc / metabolism |
| IF | 3.998 |
| 引用数 | 12 |
| WOS 分野 | BIOCHEMISTRY & MOLECULAR BIOLOGY |
| オルトメトリクス指標 |
オルトメトリクス指標項目
|
| 最多言及媒体 | Patent(IFI CLAIMS) |
| 各媒体での言及数の合計 | 4 |
| 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 | |
| 遺伝子材料 | Genomic DNA of Clostridium histolyticum JCM 1403T (JGD08942) |
| 一般微生物 | |