Competition between Sec- and TAT-dependent protein translocation in Escherichia coli

被引:220
作者
Cristóbal, S
de Gier, JW
Nielsen, H
von Heijne, G [1 ]
机构
[1] Univ Stockholm, Dept Biochem, S-10691 Stockholm, Sweden
[2] Tech Univ Denmark, Dept Biotechnol, Ctr Biol Sequence Anal, DK-2800 Lyngby, Denmark
关键词
membrane protein; protein secretion; Sec pathway; TAT pathway;
D O I
10.1093/emboj/18.11.2982
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Recently, a new protein translocation pathway, the twin-arginine translocation (TAT) pathway, has been identified in both bacteria and chloroplasts. To study the possible competition between the TAT- and the well-characterized Sec translocon-dependent pathways in Escherichia coli, we have fused the TorA TAT-targeting signal peptide to the Sec-dependent inner membrane protein leader peptidase (Lep). We find that the soluble, periplasmic P2 domain from Lep is re-routed by the TorA signal peptide into the TAT pathway, In contrast, the full-length TorA-Lep fusion protein is not re-routed into the TAT pathway, suggesting that Sec-targeting signals in Lep can override TAT-targeting information in the TorA signal peptide. We also show that the TorA signal peptide can be converted into a Sec-targeting signal peptide by increasing the hydrophobicity of its h-region, Thus, beyond the twin-arginine motif, the overall hydrophobicity of the signal peptide plays an important role in TAT versus Sec targeting, This is consistent with statistical data showing that TAT-targeting signal peptides in general have less hydrophobic h-regions than Sec-targeting signal peptides.
引用
收藏
页码:2982 / 2990
页数:9
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