Substrate-triggered position-switching of TatA and TatB is an essential step in the Escherichia coli Tat protein export pathway
Substrate-triggered position-switching of TatA and TatB is an essential step in the Escherichia coli Tat protein export pathway
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底物触发的 TatA 和 TatB 位置转换是大肠杆菌 Tat 蛋白输出途径中的重要步骤
DOI：
10.1101/113985
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发表时间：
2017
期刊：
影响因子：
--
通讯作者：
T. Palmer
中科院分区：
文献类型：
--
作者：
Johann Habersetzer;Kristoffer Moore;J. Cherry;G. Buchanan;P. Stansfeld;T. Palmer
The twin arginine protein transport (Tat) machinery mediates the translocation of folded proteins across the cytoplasmic membrane of prokaryotes and the thylakoid membrane of plant chloroplasts. The Escherichia coli Tat system comprises TatC and two additional sequence-related proteins, TatA and TatB. Here we use disulfide crosslinking and molecular modelling to show there are two binding sites for TatA/B proteins on TatC. TatA and TatB are each able to occupy both sites if they are the only TatA/B protein present. However, under resting conditions the sites are differentially occupied with TatB occupying the ‘polar cluster’ site while TatA binds adjacently at the TatC transmembrane helix 6 binding site. When the Tat system is activated by the overproduction of a substrate, TatA and TatB switch their binding sites. We propose that this substrate-triggered positional exchange is a key step in the assembly of an active Tat translocase.
影响因子：
16.6
作者：
Bluemmel, Anne-Sophie;Haag, Laura A.;Eimer, Ekaterina;Mueller, Matthias;Froebel, Julia
通讯作者：
Froebel, Julia
影响因子：
3.7
作者：
Rose P;Fröbel J;Graumann PL;Müller M
通讯作者：
Müller M
影响因子：
3.6
作者：
Fritsch MJ;Krehenbrink M;Tarry MJ;Berks BC;Palmer T
通讯作者：
Palmer T