Structural Basis for TatA Oligomerization: An NMR Study of Escherichia   coli TatA Dimeric Structure

doi:10.1371/journal.pone.0103157

CORC > 北京大学 > 化学与分子工程学院

	Structural Basis for TatA Oligomerization: An NMR Study of Escherichia coli TatA Dimeric Structure
	Zhang, Yi ; Hu, Yunfei ; Li, Hongwei ; Jin, Changwen
刊名	plos one
	2014
关键词	PROTEIN-TRANSPORT SYSTEM TWIN-ARGININE TRANSLOCASE BACILLUS-SUBTILIS DIPOLAR COUPLINGS CHEMICAL-SHIFT COMPONENT MEMBRANE COMPLEX FORM IDENTIFICATION
DOI	10.1371/journal.pone.0103157
英文摘要	Many proteins are transported across lipid membranes by protein translocation systems in living cells. The twin-arginine transport (Tat) system identified in bacteria and plant chloroplasts is a unique system that transports proteins across membranes in their fully-folded states. Up to date, the detailed molecular mechanism of this process remains largely unclear. The Escherichia coli Tat system consists of three essential transmembrane proteins: TatA, TatB and TatC. Among them, TatB and TatC form a tight complex and function in substrate recognition. The major component TatA contains a single transmembrane helix followed by an amphipathic helix, and is suggested to form the translocation pore via self-oligomerization. Since the TatA oligomer has to accommodate substrate proteins of various sizes and shapes, the process of its assembly stands essential for understanding the translocation mechanism. A structure model of TatA oligomer was recently proposed based on NMR and EPR observations, revealing contacts between the transmembrane helices from adjacent subunits. Herein we report the construction and stabilization of a dimeric TatA, as well as the structure determination by solution NMR spectroscopy. In addition to more extensive inter-subunit contacts between the transmembrane helices, we were also able to observe interactions between neighbouring amphipathic helices. The side-by-side packing of the amphipathic helices extends the solvent-exposed hydrophilic surface of the protein, which might be favourable for interactions with substrate proteins. The dimeric TatA structure offers more detailed information of TatA oligomeric interface and provides new insights on Tat translocation mechanism.; Multidisciplinary Sciences; SCI(E); PubMed; 1; ARTICLE; yunfei@pku.edu.cn; changwen@pku.edu.cn; 8; e103157; 9
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/162433]
专题	化学与分子工程学院生命科学学院
推荐引用方式 GB/T 7714	Zhang, Yi,Hu, Yunfei,Li, Hongwei,et al. Structural Basis for TatA Oligomerization: An NMR Study of Escherichia coli TatA Dimeric Structure[J]. plos one,2014.
APA	Zhang, Yi,Hu, Yunfei,Li, Hongwei,&Jin, Changwen.(2014).Structural Basis for TatA Oligomerization: An NMR Study of Escherichia coli TatA Dimeric Structure.plos one.
MLA	Zhang, Yi,et al."Structural Basis for TatA Oligomerization: An NMR Study of Escherichia coli TatA Dimeric Structure".plos one (2014).