Peptide translocation across MOMP, the major outer membrane channel from Campylobacter jejuni
| Autor: | Naresh N. Dhanasekar, Jean-Michel Bolla, Soumeya Aliouane, Mathias Winterhalter, Jean-Marie Pagès |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Biophysics Peptide Biology Single-channel medicine.disease_cause Biochemistry Campylobacter jejuni Lipid bilayer lcsh:Biochemistry 03 medical and health sciences medicine lcsh:QD415-436 lcsh:QH301-705.5 chemistry.chemical_classification Membrane potential 030102 biochemistry & molecular biology Campylobacter Residence time biology.organism_classification bacterial infections and mycoses 030104 developmental biology Membrane chemistry lcsh:Biology (General) Porin MOMP Bacterial outer membrane Research Article |
| Zdroj: | Biochemistry and Biophysics Reports, Vol 11, Iss C, Pp 79-83 (2017) Biochemistry and Biophysics Reports |
| ISSN: | 2405-5808 |
| Popis: | Here we report on translocation of short poly-arginines across the MOMP porin, the major outer membrane protein in the cell wall of Campylobacter jejuni. MOMP was purified to homogeneity from a pathogenic strain of C. jejuni. Its reconstitution in lipid membranes and measuring the ion-current revealed two main distinct populations of protein channels which we interpreted as mono and trimers. Addition of poly-arginines causes concentration and voltage dependent ion-current fluctuations. Increasing the transmembrane potential decreases the residence time of the peptide inside the channel indicating successful translocation. We conclude that poly-arginines can cross the outer membrane of Campylobacter through the MOMP channel. Highlights • Translocation of short poly-arginines across the MOMP channel has been determined. • Penta-arginine and Hepta-arginine translocate across the MOMP channel. • Voltage dependent kinetics to distinguish binding from translocation. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|