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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
ISSN1742-464X
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
DOI10.1111/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
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被引频次:8[WOS]   [WOS记录]     [WOS相关记录]
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
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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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