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dc.contributor.authorMcNeilage, Robert-
dc.date.accessioned2023-09-20T02:38:08Z-
dc.date.available2023-09-20T02:38:08Z-
dc.date.issued2023-
dc.identifier.otherOER000002342vi
dc.identifier.urihttp://dlib.hust.edu.vn/handle/HUST/23184-
dc.description.abstractThe Tat pathway is essential for photosynthetic protein transport across plant thylakoid membranes and is also ubiquitous throughout prokaryotes and archaea. The Tat pathway is quite unique amongst protein translocation pathways as it specializes in transporting folded proteins driven by a proton motive force. Mechanistic details of the actual translocation step (s) of the pathway remain elusive. Here, we show that membrane thinning stimulates Tat transport and, conversely, membrane strengthening abolishes Tat transport. We draw parallels from the Tat machinery to cell penetrating peptides and propose that the Tat pore could be toroidal, as in most pores formed by cell penetrating peptides.vi
dc.description.urihttps://www.biorxiv.org/content/10.1101/2023.07.08.548235v1.full.pdf+htmlvi
dc.formatPDFvi
dc.language.isoenvi
dc.publisherbioRxivvi
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Vietnam*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/vn/*
dc.subjectVận chuyển proteinvi
dc.subjectchuyển vị képvi
dc.subjectlỗ hình xuyếnvi
dc.subjectTwin-argininevi
dc.subjecttế bàovi
dc.subjectlỗ chân lôngvi
dc.subject.lccQH324.2vi
dc.titleCell-penetrating peptides stimulate protein transport on the Twin-arginine translocation pathway: evidence for a membrane thinning and toroidal pore mechanismvi
dc.typeJournal Articlevi
dc.description.noteCC BY-ND 4.0vi
Appears in Collections:OER - Kỹ thuật hóa học; Công nghệ sinh học - Thực phẩm; Công nghệ môi trường

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