Twin-arginine-dependent translocation of SufI in the absence of cytosolic helper proteins

Eva Holzapfel, Michael Moser, Emile Schiltz, Takuya Ueda, Jean Michel Betton, Matthias Muller*

*この研究の対応する著者

研究成果: Article査読

13 被引用数 (Scopus)

抄録

The twin-arginine translocation (Tat) machinery present in bacterial and thylakoidal membranes is able to transport fully folded proteins. Folding of some Tat precursor proteins requires dedicated chaperones that also sequester the signal sequence during the maturation process.Whether or not signal sequence-binding chaperones are a general prerequisite for all Tat substrate proteins is not known. Here, we have studied the propensity of Tat signal sequences of Escherichia coli to interact with general chaperones and peptidyl-prolyl-cis, trans-isomerases. Site-specific photocross-linking revealed a clear specificity for FK506-binding proteins. Nevertheless transport of the Tat substrate SufI into inverted inner membrane vesicles of E. coli was found to occur in the bona fide absence of any cytosolic chaperone. Our results suggest that in E. coli, cytosolic chaperones are not essential for the twin-arginine-dependent export of cofactor-less substrates.

本文言語English
ページ(範囲)5096-5105
ページ数10
ジャーナルBiochemistry
48
23
DOI
出版ステータスPublished - 2009 6月 16
外部発表はい

ASJC Scopus subject areas

  • 生化学

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