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|Title: ||The Preprotein Binding Domain of SecA Displays Intrinsic Rotational Dynamics|
|Authors: ||Vandenberk, Niels|
Portaliou, Athina G.
|Issue Date: ||2019|
|Publisher: ||CELL PRESS|
|Citation: ||STRUCTURE, 27 (1), p. 90-101|
|Abstract: ||SecA converts ATP energy to protein translocation work. Together with the membrane-embedded SecY channel it forms the bacterial protein translocase. How secretory proteins bind to SecA and drive conformational cascades to promote their secretion remains unknown. To address this, we focus on the preprotein binding domain (PBD) of SecA. PBD crystalizes in three distinct states, swiveling around its narrow stem. Here, we examined whether PBD displays intrinsic dynamics in solution using single-molecule Forster resonance energy transfer (smFRET). Unique cysteinyl pairs on PBD and apposed domains were labeled with donor/acceptor dyes. Derivatives were analyzed using pulsed interleaved excitation and multi-parameter fluorescence detection. The PBD undergoes significant rotational motions, occupying at least three distinct states in dimeric and four in monomeric soluble SecA. Nucleotides do not affect smFRET-detectable PBD dynamics. These findings lay the foundations for single-molecule dissection of translocase mechanics and suggest models for possible PBD involvement during catalysis.|
|Notes: ||[Vandenberk, Niels; Hofkens, Johan; Hendrix, Jelle] Katholieke Univ Leuven, Dept Chem, Div Mol Imaging & Photon, Lab Photochem & Spect, Celestijnenlaan 200F, B-3001 Leuven, Belgium. [Karamanou, Spyridoula; Portaliou, Athina G.; Zorzini, Valentina; Economou, Anastassios] Katholieke Univ Leuven, Dept Microbiol & Immunol, Rega Inst Med Res, Lab Mol Bacteriol, Herestraat 49,Gasthuisberg Campus, B-3000 Leuven, Belgium. [Hendrix, Jelle] Hasselt Univ, Dynam Bioimaging Lab, Adv Opt Microscopy Ctr, Biomed Res Inst, Agoralaan C BIOMED, B-3590 Diepenbeek, Belgium.
|ISI #: ||000454804900009|
|Type: ||Journal Contribution|
|Appears in Collections: ||Research publications|
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