Monitoring the binding and insertion of a single transmembrane protein by an insertase

Pawel R. Laskowski, Kristyna Pluhackova, Maximilian Haase, Brian M. Lang, Gisela Nagler, Andreas Kuhn and Daniel J. Müller ()
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Pawel R. Laskowski: ETH Zurich
Kristyna Pluhackova: ETH Zurich
Maximilian Haase: Universität Hohenheim
Brian M. Lang: ETH Zurich
Gisela Nagler: Universität Hohenheim
Andreas Kuhn: Universität Hohenheim
Daniel J. Müller: ETH Zurich

Nature Communications, 2021, vol. 12, issue 1, 1-11

Abstract: Abstract Cells employ highly conserved families of insertases and translocases to insert and fold proteins into membranes. How insertases insert and fold membrane proteins is not fully known. To investigate how the bacterial insertase YidC facilitates this process, we here combine single-molecule force spectroscopy and fluorescence spectroscopy approaches, and molecular dynamics simulations. We observe that within 2 ms, the cytoplasmic α-helical hairpin of YidC binds the polypeptide of the membrane protein Pf3 at high conformational variability and kinetic stability. Within 52 ms, YidC strengthens its binding to the substrate and uses the cytoplasmic α-helical hairpin domain and hydrophilic groove to transfer Pf3 to the membrane-inserted, folded state. In this inserted state, Pf3 exposes low conformational variability such as typical for transmembrane α-helical proteins. The presence of YidC homologues in all domains of life gives our mechanistic insight into insertase-mediated membrane protein binding and insertion general relevance for membrane protein biogenesis.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-27315-3

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DOI: 10.1038/s41467-021-27315-3

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