日本語
 
Help Privacy Policy ポリシー/免責事項
  詳細検索ブラウズ

アイテム詳細

登録内容を編集ファイル形式で保存
一時保存へ追加
 タグ情報を表示リリース履歴を表示詳細要約
  Yersinia enterocolitica type III secretion: Evidence for the ability to transport proteins that are folded prior to secretion

Wilharm, G., Lehmann, V., Neumayer, W., & Trček, J. (2004). Yersinia enterocolitica type III secretion: Evidence for the ability to transport proteins that are folded prior to secretion. BMC Microbiology, 4, 27-27. doi:10.1186/1471-2180-4-27.

Item is

 

表示: 全項目 非表示: 全項目

基本情報

表示: 非表示:
アイテムのパーマリンク: https://hdl.handle.net/11858/00-001M-0000-0010-882C-F 版のパーマリンク: https://hdl.handle.net/11858/00-001M-0000-0010-882D-D
資料種別: 学術論文
その他のタイトル : BMC Microbiol

ファイル

表示: ファイル

関連URL

表示:

作成者

表示:
非表示:
 作成者:
Wilharm, Gottfried, 著者
Lehmann, Verena1, 著者
Neumayer, Wibke, 著者
Trček, Janja, 著者
所属:
1Max Planck Society, ou_persistent13              

内容説明

表示:
非表示:
キーワード: -
 要旨: Background Pathogenic Yersinia species (Y. enterocolitica, Y. pestis, Y. pseudotuberculosis) share a type three secretion system (TTSS) which allows translocation of effector proteins (called Yops) into host cells. It is believed that proteins are delivered through a hollow needle with an inner diameter of 2–3 nm. Thus transport seems to require substrates which are essentially unfolded. Recent work from different groups suggests that the Yersinia TTSS cannot accommodate substrates which are folded prior to secretion. It was suggested that folding is prevented either by co-translational secretion or by the assistance of specific Yop chaperones (called Sycs). Results In this study we have fused YopE secretion signals of various length to the mouse dihydrofolate reductase (DHFR) in order to analyse the DHFR folding state prior to secretion. We could demonstrate that secretion-deficient as well as secretion-competent YopE-DHFR fusions complexed to SycE can be efficiently purified from Yersinia cytosol by affinity chromatography using methotrexate-agarose. This implies the folding of the DHFR fusion moiety despite SycE binding and contradicts the previously presented model of folding inhibition by chaperone binding. Secretion-deficient YopE-DHFR fusions caused severe jamming of the TTSS. This observation contradicts the co-translational secretion model. Conclusions We present evidence that the Yersinia TTSS is familiar with the processing of transport substrates which are folded prior to secretion. We therefore predict that an unfoldase is involved in type III secretion.

資料詳細

表示:
非表示:
言語: eng - English
 日付: 2004-07
 出版の状態: 出版
 ページ: -
 出版情報: -
 目次: -
 査読: -
 識別子（DOI, ISBNなど）: eDoc: 230978
DOI: 10.1186/1471-2180-4-27
 学位: -

関連イベント

表示:

訴訟

表示:

Project information

表示:

出版物 1

表示:
非表示:
出版物名: BMC Microbiology
  出版物の別名 : BMC Microbiol
種別: 学術雑誌
 著者・編者:
所属:
出版社, 出版地: -
ページ: - 巻号: 4 通巻号: - 開始・終了ページ: 27 - 27 識別子（ISBN, ISSN, DOIなど）: ISSN: 1471-2180