Role of the N-terminal signal peptide in the membrane insertion of Aquifex aeolicus F1F0 ATP synthase c-subunit

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	Role of the N-terminal signal peptide in the membrane insertion of Aquifex aeolicus F1F0 ATP synthase c-subunit
	Zhang, Chunli 1; Marcia, Marco 2; Langer, Julian D.1; Peng, Guohong 1,3; Michel, Hartmut 1
刊名	FEBS JOURNAL
	2013-07-01
卷号	280 期号:14 页码:3425-3435
关键词	energy conservation membrane insertion membrane topology rotary ATPases signal peptide
ISSN号	1742-464X
通讯作者	Peng, GH
中文摘要	Rotary ATPases are membrane protein complexes that couple ATP hydrolysis to ion translocation across the membrane. Overall, they are evolutionarily well conserved, but the N-terminal segments of their rotary subunits (c-subunits) possess different lengths and levels of hydrophobicity across species. By analyzing the N-terminal variability, we distinguish four phylogenetic groups of c-subunits (groups 1-4). We characterize a member of group 2, the c-subunit from Aquifexaeolicus F1F0 ATP synthase, both in native cells and in a heterologous expression system. We demonstrate that its N-terminal segment forms a signal peptide with signal recognition particle (SRP) recognition features and is obligatorily required for membrane insertion. Based on our study and on previous characterizations of c-subunits from other organisms, we propose that c-subunits follow different membrane insertion pathways.
英文摘要	Rotary ATPases are membrane protein complexes that couple ATP hydrolysis to ion translocation across the membrane. Overall, they are evolutionarily well conserved, but the N-terminal segments of their rotary subunits (c-subunits) possess different lengths and levels of hydrophobicity across species. By analyzing the N-terminal variability, we distinguish four phylogenetic groups of c-subunits (groups 1-4). We characterize a member of group 2, the c-subunit from Aquifexaeolicus F1F0 ATP synthase, both in native cells and in a heterologous expression system. We demonstrate that its N-terminal segment forms a signal peptide with signal recognition particle (SRP) recognition features and is obligatorily required for membrane insertion. Based on our study and on previous characterizations of c-subunits from other organisms, we propose that c-subunits follow different membrane insertion pathways.
学科主题	Biochemistry & Molecular Biology
WOS标题词	Science & Technology ; Life Sciences & Biomedicine
类目[WOS]	Biochemistry & Molecular Biology
研究领域[WOS]	Biochemistry & Molecular Biology
关键词[WOS]	SEQUENCE CLEAVAGE SITES ; ESCHERICHIA-COLI ; INNER MEMBRANE ; ROTOR RING ; PROTEIN TRANSLOCATION ; RECOGNITION PARTICLE ; THERMUS-THERMOPHILUS ; PROTEOLIPID SUBUNIT ; TARGETING PATHWAYS ; COMPLETE GENOME
收录类别	SCI
原文出处	10.1111/febs.12336
语种	英语
WOS记录号	WOS:000327128700022
公开日期	2014-07-17
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/16622]
专题	海洋研究所_实验海洋生物学重点实验室
作者单位	1.Max Planck Inst Biophys, Dept Mol Membrane Biol, D-60438 Frankfurt, Germany 2.Yale Univ, Dept Mol Cellular & Dev Biol, New Haven, CT USA 3.Chinese Acad Sci, Inst Oceanol, Qingdao, Peoples R China
推荐引用方式 GB/T 7714	Zhang, Chunli,Marcia, Marco,Langer, Julian D.,et al. Role of the N-terminal signal peptide in the membrane insertion of Aquifex aeolicus F1F0 ATP synthase c-subunit[J]. FEBS JOURNAL,2013,280(14):3425-3435.
APA	Zhang, Chunli,Marcia, Marco,Langer, Julian D.,Peng, Guohong,&Michel, Hartmut.(2013).Role of the N-terminal signal peptide in the membrane insertion of Aquifex aeolicus F1F0 ATP synthase c-subunit.FEBS JOURNAL,280(14),3425-3435.
MLA	Zhang, Chunli,et al."Role of the N-terminal signal peptide in the membrane insertion of Aquifex aeolicus F1F0 ATP synthase c-subunit".FEBS JOURNAL 280.14(2013):3425-3435.