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© Valérie Choumet
Mosquitoes were orally infected with the chikungunya virus. Midguts were dissected at day 5 post-infection, fixed and permeabilised. Virus is shown in red (anti-E2 protein, cyanine 3), the actin network in green (phalloidin 548) and nuclei in blue (DAPI).
Publication : Biochemistry

NMR conformational study of the cytoplasmic domain of the canine Sec61 gamma protein from the protein translocation pore of the endoplasmic reticulum membrane

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Biochemistry - 26 Nov 1996

Beswick V, Baleux F, Huynh-Dinh T, Képès F, Neumann JM, Sanson A

Link to Pubmed [PMID] – 8942632

Biochemistry 1996 Nov;35(47):14717-24

Conformational studies of the synthesized N-terminal cytoplasmic domain of the canine Sec61 gamma protein, an essential protein from the translocation pore of secretory proteins across the endoplasmic reticulum membrane, were performed using two-dimensional proton NMR spectroscopy. This canine domain is one of the smallest domains within the homologous protein family and may thus constitute the minimal functional structure. The peptide was solubilized in pure aqueous solution or in the presence of dodecylphosphocholine micelles mimicking a membrane-solution interface. In pure aqueous solution, the peptide is remarkably unfolded. Forming a stable complex with dodecylphosphocholine micelles, it acquires a well-defined alpha-helix-loop-alpha-helix secondary structure, with the helix, highly amphipathic, lying at the micelle surface. The loop comprising four residues is delimited by two flanking helix-capping structures, highly conserved in the whole homologous protein family. No tertiary structure, which could have been revealed by interhelix NOE contacts, was observed. From these experimental results and using general arguments based on sequence information and knowledge of peptide-membrane interactions, a structure of the entire Sec61 gamma protein in membrane bilayers is proposed.

http://www.ncbi.nlm.nih.gov/pubmed/8942632