Downloads: 141

Files in This Item:
File Description SizeFormat 
j.bbrc.2012.07.097.pdf614.85 kBAdobe PDFView/Open
Title: Eicosapentaenoic acid facilitates the folding of an outer membrane protein of the psychrotrophic bacterium, Shewanella livingstonensis Ac10.
Authors: Dai, Xian-Zhu
Kawamoto, Jun
Sato, Satoshi B
Esaki, Nobuyoshi  KAKEN_id
Kurihara, Tatsuo  kyouindb  KAKEN_id  orcid (unconfirmed)
Author's alias: 栗原, 達夫
Keywords: Eicosapentaenoic acid
Membrane protein
Protein folding
Cold-adaptation mechanism
Issue Date: 24-Aug-2012
Publisher: Elsevier Inc.
Journal title: Biochemical and biophysical research communications
Volume: 425
Issue: 2
Start page: 363
End page: 367
Abstract: Polyunsaturated fatty acids, such as eicosapentaenoic acid (EPA), are found in various cold-adapted microorganisms. We previously demonstrated that EPA-containing phospholipids (EPA-PLs) synthesized by the psychrotrophic bacterium Shewanella livingstonensis Ac10 support cell division, membrane biogenesis, and the production of membrane proteins at low temperatures. In this article, we demonstrate the effects of EPA-PLs on the folding and conformational transition of Omp74, a major outer membrane cold-inducible protein in this bacterium. Omp74 from an EPA-less mutant migrated differently from that of the parent strain on SDS-polyacrylamide gel, suggesting that EPA-PLs affect the conformation of Omp74 in vivo. To examine the effects of EPA-PLs on Omp74 protein folding, in vitro refolding of recombinant Omp74 was carried out with liposomes composed of 1, 2-dipalmitoleoyl-sn-glycero-3-phosphoglycerol and 1, 2-dipalmitoleoyl-sn-glycero-3-phosphoethanolamine (1:1molar ratio) with or without EPA-PLs as guest lipids. SDS-PAGE analysis of liposome-reconstituted Omp74 revealed more rapid folding in the presence of EPA-PLs. CD spectroscopy of Omp74 folding kinetics at 4°C showed that EPA-PLs accelerated β-sheet formation. These results suggest that EPA-PLs act as chemical chaperones, accelerating membrane insertion and secondary structure formation of Omp74 at low temperatures.
Rights: © 2012 Elsevier Inc.
This is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。
DOI(Published Version): 10.1016/j.bbrc.2012.07.097
PubMed ID: 22842563
Appears in Collections:Journal Articles

Show full item record

Export to RefWorks

Export Format: 

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.