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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Opposite Effects of Lysophosphatidylethanolamines on Conformation of OmpF-like Porin from Yersinia pseudotuberculosis

Author(s): Ludmila A. Davydova, Nina M. Sanina, Olga D. Novikova, Olga Y. Portnyagina, Svetlana I. Bakholdina, Peter V. Velansky, Natalia S. Vorobyeva, Valentina A. Khomenko, Valery L. Shnyrov and Mikhail V. Bogdanov

Volume 22 , Issue 12 , 2015

Page: [1060 - 1065] Pages: 6

DOI: 10.2174/0929866522666150909141052

Price: $65

Abstract

Lysophosphatidyletnolamine (LPE) is one of enigmatic lipids of bacteria. It is generated from major membrane lipid - phosphatidylethanolamine at severe changes of the bacterial growth conditions. Accumulation of this phospholipid in cells of Gram-negative enterobacterium Yersinia pseudotuberculosis results in the enhanced thermostability of OmpF-like porin (YOmpF) from the same bacteria. The respective integral conformational rearrangements may disturb the channel permeability of protein under stress conditions. However, role of fatty acid composition of LPE in this effect remained unclear. Present work demonstrated that the level of unsaturated LPE is 3.5 times higher than saturated one in total LPE of bacterial cells exposed to stress (phenol treatment). Unsaturated 1-oleoyl-2-hydroxy-sn-glycero-3-phosphoethanolamine (MOPE) and saturated LPE 1-palmitoyl-2- hydroxy-sn-glycero-3-phosphoethanolamine (MPPE) oppositely affect the conformation of YOmpF. MOPE increases the protein thermal stability due to more dense packing of monomers in porin and preserves its trimeric form at elevated temperature, while MPPE weakens the contact between monomers and promotes dissociation of the protein.

Keywords: Lipid-protein interactions; gas-liquid chromatography; differential scanning calorimetry; intrinsic protein fluorescence; Western blotting.

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