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
  Phage P4 origin-binding domain structure reveals a mechanism for regulation of DNA-binding activity by homo- and heterodimerization of winged helix proteins

Yeo, H.-J., Ziegelin, G., Korolev, S., Calendar, R., Lanka, E., & Waksman, G. (2002). Phage P4 origin-binding domain structure reveals a mechanism for regulation of DNA-binding activity by homo- and heterodimerization of winged helix proteins. Molecular Microbiology, 43(4), 855-867.

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-0000-0010-8C28-2 版のパーマリンク: https://hdl.handle.net/11858/00-001M-0000-0010-8C29-F
資料種別: 学術論文
その他のタイトル : Mol 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:
Yeo, Hye-Jeong, 著者
Ziegelin, Günter1, 著者
Korolev, Sergey, 著者
Calendar, Richard, 著者
Lanka, Erich1, 著者
Waksman, Gabriel, 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: The origin-binding domain of the gp protein of phage P4 (P4-OBD) mediates origin recognition and regulation of gp activity by the protein Cnr. We have determined the crystal structure of P4-OBD at 2.95 Å resolution. The structure of P4-OBD is that of a dimer with pseudo twofold symmetry. Each subunit has a winged helix topology with a unique structure among initiator proteins. The only structural homologue of the P4-OBD subunit is the DNA-binding domain of the eukaryotic transcriptional activator Rfx1. Based on this structural alignment, a model for origin recognition by the P4-OBD dimer is suggested. P4-OBD mutations that interfere with Cnr binding locate to the dimer interface, indicating that Cnr acts by disrupting the gp dimer. P4-OBD dimerization is mediated by helices 1 and 3 in both subunits, a mode of winged helix protein dimerization that is reminiscent of that of the eukaryotic transcription factors E2F and DP. This, in turn, suggests that Cnr is also a winged helix protein, a possibility that is supported by previously unreported sequence homologies between Cnr and Rfx1 and homology modelling. Hence, in a mechanism that appears to be conserved from phage to man, the DNA-binding activity of winged helix proteins can be regulated by other winged helix proteins via the versatile use of the winged helix motif as a homo- or heterodimerization scaffold.

資料詳細

表示:
非表示:
言語: eng - English
 日付: 2002-03-27
 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: 24569
 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: Molecular Microbiology
  出版物の別名 : Mol Microbiol
種別: 学術雑誌
 著者・編者:
所属:
出版社, 出版地: -
ページ: - 巻号: 43 (4) 通巻号: - 開始・終了ページ: 855 - 867 識別子（ISBN, ISSN, DOIなど）: -