Elucidating the Native Architecture of the YidC: Ribosome ComplexKedrov, A., Sustarsic, M., de Keyzer, J., Caumanns, J. J., Wu, Z. C. & Driessen, A. J. M., 15-Nov-2013, In : Journal of Molecular Biology. 425, 22, p. 4112-4124 13 p.
Research output: Contribution to journal › Article › Academic › peer-review
Membrane protein biogenesis in bacteria occurs via dedicated molecular systems SecYEG and YidC that function independently and in cooperation. YidC belongs to the universally conserved Oxal/Alb3/YidC family of membrane insertases and is believed to associate with translating ribosomes at the membrane surface. Here, we have examined the architecture of the YidC:ribosome complex formed upon YidC-mediated membrane protein insertion. Fluorescence correlation spectroscopy was employed to investigate the complex assembly under physiological conditions. A slightly acidic environment stimulates binding of detergent-solubilized YidC to ribosomes due to electrostatic interactions, while YidC acquires specificity for translating ribosomes at pH-neutral conditions. The nanodisc reconstitution of the YidC to embed it into a native phospholipid membrane environment strongly enhances the YidC: ribosome complex formation. A single copy of YidC suffices for the binding of translating ribosome both in detergent and at the lipid membrane interface, thus being the minimal functional unit. Data reveal molecular details on the insertase functioning and interactions and suggest a new structural model for the YidC:ribosome complex. (C) 2013 The Authors. Published by Elsevier Ltd. All rights reserved.
|Number of pages||13|
|Journal||Journal of Molecular Biology|
|Publication status||Published - 15-Nov-2013|
- macromolecular assembly, membrane protein, membrane insertase, single-molecule biophysics, ribosome, ESCHERICHIA-COLI YIDC, PHOSPHOLIPID-BILAYER NANODISCS, CROSS-CORRELATION SPECTROSCOPY, SIGNAL RECOGNITION PARTICLE, POLYTOPIC MEMBRANE-PROTEINS, SECYEG TRANSLOCON, INSERTION, BIOGENESIS, BINDING, OXA1