Related ArticlesSolid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106.
Chem Phys Lipids. 2013 Sep 24;
Authors: Zhang L, Liu L, Maltsev S, Lorigan GA, Dabney-Smith C
Abstract
The chloroplast twin arginine translocation system transports highly folded precursor proteins across the thylakoid using the protonmotive force as its only energy source. Hcf106 and another thylakoid protein, cpTatC compose the precursor receptor complex. Hcf106 is predicted to contain a single amino terminal transmembrane domain (TMD) followed by a Pro-Gly hinge, an amphipathic ?-helix, and a loosely structured carboxy terminus. Hcf106 has been shown biochemically to insert spontaneously into thylakoid membranes; however, how this occurs is not understood. To investigate how Hcf106 inserts itself into the membrane unassisted, solid-state NMR spectroscopy was used to investigate the membrane activity of the TMD. A synthetic peptide of the Hcf106 TMD was incorporated into multilamellar vesicles made of 100% 1-palmitoyl-2-oleoyl-sn-glycero-phosphocholine (POPC) or 85%:15% ratio with monogalactosyl diacylglycerol (POPC/MGDG) to probe peptide-lipid interaction. Solid-state (31)P NMR and (2)H NMR spectroscopic techniques were used to reveal peptide perturbations of the phospholipid membranes. Changes in spectral lineshape, chemical shift anisotropy width, (31)P T1 relaxation time and SCD order parameters demonstrated that the Hcf106 TMD peptide interacted with the phospholipids. Furthermore, the comparison between POPC and POPC/MGDG multilamellar vesicles indicated that lipid bilayer composition affected the peptide-lipid interaction with the peptide interacting preferentially with vesicles that more closely mimic the thylakoid.
PMID: 24075840 [PubMed - as supplied by publisher]
Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106
Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106
Publication date: Available online 24 September 2013
Source:Chemistry and Physics of Lipids</br>
Author(s): Lei Zhang , Lishan Liu , Sergey Maltsev , Gary A. Lorigan , Carole Dabney-Smith</br>
The chloroplast twin arginine translocation system transports highly folded precursor proteins across the thylakoid using the protonmotive force as its only energy source. Hcf106 and another thylakoid protein, cpTatC compose the precursor receptor...
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Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106.
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