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Structure-based working model of SecDF, a proton-driven bacterial protein translocation factor

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dc.contributor.author Tsukazaki, Tomoya en
dc.date.accessioned 2018-10-23T00:46:58Z en
dc.date.available 2018-10-23T00:46:58Z en
dc.date.issued 2018-04-27 en
dc.identifier.issn 0378-1097 en
dc.identifier.uri http://hdl.handle.net/10061/12603 en
dc.description.abstract The bacterial membrane protein SecDF enhances protein translocation across the membrane driven by the complex of SecA ATPase and SecYEG. Many newly synthesized proteins in the cytoplasm are programmed to be translocated to the periplasm via the narrow channel that is formed in the center of SecYEG. During the protein-translocation process, SecDF is proposed to undergo repeated conformational transitions to pull out the precursor protein from the SecYEG channel into the periplasm. Once SecDF captures the precursor protein on the periplasmic surface, SecDF can complete protein translocation even if SecA function is inactivated by ATP depletion, implying that SecDF is a protein-translocation motor that works independent of SecA. Structural and functional analyses of SecDF in 2011 suggested that SecDF utilizes the proton gradient and interacts with precursor protein in the flexible periplasmic region. The crystal structures of SecDF in different states at more than 3Å resolution were reported in 2017 and 2018, which further improved our understanding of the dynamic molecular mechanisms of SecDF. This review summarizes recent structural studies of SecDF. ja
dc.language.iso en en
dc.publisher Oxford University Press en
dc.rights © 2018 Federation of European Microbiological Societies ja
dc.rights This is a pre-copyedited, author-produced version of an article accepted for publication in [FEMS Microbiology Letters] following peer review. The version of record [FEMS Microbiology Letters, 365(12), fny112] is available online at: https://doi.org/10.1093/femsle/fny112 en
dc.rights 出版社許諾条件により、本文は2019年4月27日以降に公開 ja
dc.subject protein translocation en
dc.subject SecDF en
dc.subject SecYEG en
dc.subject crystal structure en
dc.subject proton driven en
dc.title Structure-based working model of SecDF, a proton-driven bacterial protein translocation factor en
dc.type.nii Journal Article en
dc.contributor.transcription ツカザキ, トモヤ ja
dc.contributor.alternative 塚崎, 智也 ja
dc.textversion author en
dc.identifier.ncid AA00193861 en
dc.identifier.jtitle FEMS Microbiology Letters en
dc.identifier.volume 365 en
dc.identifier.issue 12 en
dc.relation.doi 10.1093/femsle/fny112 en
dc.identifier.artnum fny112 en
dc.identifier.NAIST-ID 73299737 en
dc.relation.pmid 29718185 en


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