Institutional Repository of Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences
Role of the N-terminal signal peptide in the membrane insertion of Aquifex aeolicus F1F0 ATP synthase c-subunit | |
Zhang, Chunli1; Marcia, Marco2; Langer, Julian D.1; Peng, Guohong1,3; Michel, Hartmut1; Peng, GH | |
2013-07-01 | |
发表期刊 | FEBS JOURNAL |
ISSN | 1742-464X |
卷号 | 280期号:14页码:3425-3435 |
文章类型 | Article |
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.; 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. |
关键词 | Energy Conservation Membrane Insertion Membrane Topology Rotary Atpases Signal Peptide |
学科领域 | Biochemistry & Molecular Biology |
DOI | 10.1111/febs.12336 |
URL | 查看原文 |
收录类别 | SCI |
语种 | 英语 |
WOS研究方向 | Biochemistry & Molecular Biology |
WOS类目 | Biochemistry & Molecular Biology |
WOS记录号 | WOS:000327128700022 |
WOS关键词 | SEQUENCE CLEAVAGE SITES ; ESCHERICHIA-COLI ; INNER MEMBRANE ; ROTOR RING ; PROTEIN TRANSLOCATION ; RECOGNITION PARTICLE ; THERMUS-THERMOPHILUS ; PROTEOLIPID SUBUNIT ; TARGETING PATHWAYS ; COMPLETE GENOME |
WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://ir.qdio.ac.cn/handle/337002/16622 |
专题 | 实验海洋生物学重点实验室 |
通讯作者 | Peng, GH |
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,&Peng, GH.(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. |
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