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Pull-and-Paste of Single Transmembrane Proteins.
Journal article

Pull-and-Paste of Single Transmembrane Proteins.

  • Serdiuk T Department of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH) Zurich , 4058 Basel, Switzerland.
  • Mari SA Department of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH) Zurich , 4058 Basel, Switzerland.
  • Müller DJ Department of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH) Zurich , 4058 Basel, Switzerland.
  • 2017-06-20
Published in:
  • Nano letters. - 2017
Membrane protein insertion and folding
YidC insertase
atomic force microscopy
folding pathway
mechanical reconstitution
single-molecule force spectroscopy
Cell Membrane
Escherichia coli Proteins
Membrane Transport Proteins
Membranes, Artificial
Models, Molecular
Monosaccharide Transport Proteins
Phospholipids
Protein Binding
Protein Conformation
Protein Folding
Protein Transport
Stress, Mechanical
Symporters
English How complex cytoplasmic membrane proteins insert and fold into cellular membranes is not fully understood. One problem is the lack of suitable approaches that allow investigating the process by which polypeptides insert and fold into membranes. Here, we introduce a method to mechanically unfold and extract a single polytopic α-helical membrane protein, the lactose permease (LacY), from a phospholipid membrane, transport the fully unfolded polypeptide to another membrane and insert and refold the polypeptide into the native structure. Insertion and refolding of LacY is facilitated by the transmembrane chaperone/insertase YidC in the absence of the SecYEG translocon. Insertion into the membrane occurs in a stepwise, stochastic manner employing multiple coexisting pathways to complete the folding process. We anticipate that our approach will provide new means of studying the insertion and folding of membrane proteins and to mechanically reconstitute membrane proteins at high spatial precision and stoichiometric control, thus allowing the functional programming of synthetic and biological membranes.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://susi.usi.ch/global/documents/238993
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