Peptidoglycan layer and disruption processes in Bacillus subtilis cells visualized using quick-freeze, deep-etch electron microscopy

• Material Type: 文書・図像類
• Title: Peptidoglycan layer and disruption processes in Bacillus subtilis cells visualized using quick-freeze, deep-etch electron microscopy
• Author/Editor: Tulum, Isil; Tahara, Yuhei O; Miyata, Makoto
• Author Heading: Tulum, Isil; Tahara, Yuhei O; Miyata, Makoto
• Publication, Distribution, etc.: Oxford University Press
• Publication Date: 2019-11-05
• Publication Date (W3CDTF): 2019-11-05
• Periodical title: Microscopy
• No. or year of volume/issue: 68 6
• Volume: 68
• Issue: 6
• Pages: 441-449
• ISSN (Periodical Title): ISSN : 2050-5701
• Text Language Code: eng
• Subject Heading: リゾチーム; 蛍光; ペニシリン; パイクラスト; L型; 膨圧; lysozyme; fluorescence; penicillin; piecrust; L-form; turgor
• Target Audience: 一般
• Note (General): Peptidoglycan, which is the main component of the bacterial cell wall, is a heterogeneous polymer of glycan strands cross-linked with short peptides and is synthesized in cooperation with the cell division cycle. Although it plays a critical role in bacterial survival, its architecture is not well understood. Herein, we visualized the architecture of the peptidoglycan surface in Bacillus subtilis at the nanometer resolution, using quick-freeze, deep-etch electron microscopy (EM). Filamentous structures were observed on the entire surface of the cell, where filaments about 11 nm wide formed concentric circles on cell poles, filaments about 13 nm wide formed a circumferential mesh-like structure on the cylindrical part and a 'piecrust' structure was observed at the boundary. When growing cells were treated with lysozyme, the entire cell mass migrated to one side and came out from the cell envelope. Fluorescence labeling showed that lysozyme preferentially bound to a cell pole and cell division site, where the peptidoglycan synthesis was not complete. Ruffling of surface structures was observed during EM. When cells were treated with penicillin, the cell mass came out from a cleft around the cell division site. Outward curvature of the protoplast at the cleft seen using EM suggested that turgor pressure was applied as the peptidoglycan was not damaged at other positions. When muropeptides were depleted, surface filaments were lost while the rod shape of the cell was maintained. These changes can be explained on the basis of the working points of the chemical structure of peptidoglycan.
• Source: http://dlisv03.media.osaka-cu.ac.jp/contents/osakacu/journal/20505701-68-6-441.pdf
• Access Restrictions: 限定公開
• Rights (production): This article has been accepted for publication in Microscopy Published by Oxford University Press. The version of record is available free of charge on Microscopy website at: https://doi.org/10.1093/jmicro/dfz033.
• Related Material (DOI): 10.1093/jmicro/dfz033
• Is Version Of (URI): https://doi.org/10.1093/jmicro/dfz033; URI
• Data Provider (Database): 国立情報学研究所 : 学術機関リポジトリデータベース（IRDB）（機関リポジトリ）; https://irdb.nii.ac.jp
• Original Data Provider (Database): 大阪市立大学 : 大阪市立大学学術機関リポジトリ