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Biochim Biophys Acta. 2015 Mar;1848(3):878-85. doi: 10.1016/j.bbamem.2014.12.014. Epub 2014 Dec 24.

Structure of the N-terminal segment of human retinol dehydrogenase 11 and its preferential lipid binding using model membranes.

Author information

1
CUO-Recherche, Hôpital du Saint-Sacrement, Centre de recherche du CHU de Québec and Département d'ophtalmologie, Faculté de médecine, and Regroupement stratégique PROTEO, Université Laval, Québec, Québec, Canada.
2
CUO-Recherche, Hôpital du Saint-Sacrement, Centre de recherche du CHU de Québec and Département d'ophtalmologie, Faculté de médecine, and Regroupement stratégique PROTEO, Université Laval, Québec, Québec, Canada. Electronic address: christian.salesse@fmed.ulaval.ca.

Abstract

Retinol dehydrogenase 11 (RDH11) has been postulated to be anchored to membranes by means of its N-terminal segment in retinal pigment epithelial (RPE) cells where it participates to the visual cycle. The analysis of the primary sequence of RDH11 revealed that its N-terminal hydrophobic segment could be involved in the anchoring of this enzyme to membranes. However, no information is yet available on the properties of this N-terminal segment to support this role. The secondary structure and membrane binding of two N-terminal peptides of RDH11 with different lengths have thus been investigated to provide this information. Online tools allowed predicting an α-helical secondary structure for both peptides. Infrared spectroscopy and circular dichroism have shown that the α-helix of the Long-peptide (35 amino acids) is longer and more rigid than that of the Short-peptide (25 amino acids) regardless of the type of solvent. Langmuir monolayers have been used as a model membrane to study lipid-peptide interactions. Values of maximum insertion pressure and synergy suggested a preferential binding of the Long-peptide to lipids with a phosphoethanolamine polar head group, which are abundant in the RPE. Furthermore, infrared spectroscopy in monolayers has shown that the α-helical structure of the Long-peptide is more stable in the presence of saturated phospholipids whereas the structure of the Short-peptide is mainly disordered. Altogether, the present data demonstrate that the α-helical hydrophobic core of the N-terminal segment of RDH11 displays properties typical of transmembrane domains, in agreement with its postulated role in the membrane anchoring of this protein.

KEYWORDS:

Maximum insertion pressure; N-terminal anchoring peptide; Protein secondary structure; Retinal pigment epithelium; Retinol dehydrogenase 11; monolayer

PMID:
25542782
DOI:
10.1016/j.bbamem.2014.12.014
[Indexed for MEDLINE]
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