Solid-state NMR investigations of peptide–lipid interactions of the transmembrane domain of a plant-derived protein, Hcf106
| Autor: | Gary A. Lorigan, Lei Zhang, Sergey Maltsev, Carole Dabney-Smith, Lishan Liu |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Receptor complex
Lipid Bilayers Molecular Sequence Data Thylakoids Biochemistry chemistry.chemical_compound Membrane activity Amino Acid Sequence Lipid bilayer Nuclear Magnetic Resonance Biomolecular Molecular Biology POPC Plant Proteins Galactolipids Vesicle Organic Chemistry technology industry and agriculture Membrane Proteins Cell Biology Protein Structure Tertiary Crystallography Transmembrane domain chemistry Thylakoid Phosphatidylcholines Biophysics lipids (amino acids peptides and proteins) Peptides Energy source |
| Zdroj: | Chemistry and Physics of Lipids. :123-130 |
| ISSN: | 0009-3084 |
| DOI: | 10.1016/j.chemphyslip.2013.09.002 |
| Popis: | 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 α-helix, and a loosely structured carboxyl 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 31P NMR and 2H NMR spectroscopic techniques were used to reveal peptide perturbations of the phospholipid membranes. Changes in spectral lineshape, chemical shift anisotropy width, 31P 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. |
| Databáze: | OpenAIRE |
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