Affinity of the periplasmic chaperone Skp ofEscherichia colifor phospholipids, lipopolysaccharides and non-native outer membrane proteins

Autor:	Martin Potgeter, Ute Schäfer, Matthias Müller, Rudy A. Demel, Jan Tommassen, Hans de Cock
Rok vydání:	1999
Předmět:	Membrane biology Chaperone (protein) Translocase of the outer membrane biology.protein Outer membrane efflux proteins Virulence-related outer membrane protein family Protein folding Periplasmic space Bacterial outer membrane Biochemistry Cell biology
Zdroj:	European Journal of Biochemistry. 259:96-103
ISSN:	1432-1033 0014-2956
Popis:	The Skp protein of Escherichia coli has been proposed to be a periplasmic molecular chaperone involved in the biogenesis of outer membrane proteins. In this study, evidence is obtained that Skp exists in two different states characterized by their different sensitivity to proteases. The conversion between these states can be modulated in vitro by phospholipids, lipopolysaccharides and bivalent cations. Skp is able to associate with and insert into phospholipid membranes in vitro, indicating that it may associate with phospholipids in the inner and/or outer membrane in vivo. In addition, it interacts specifically with outer membrane proteins that are in their non-native state. We propose that Skp is required in vivo for the efficient targeting of unfolded outer membrane proteins to the membrane.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::494369c864678fe68e5f800f4e6aea4a https://doi.org/10.1046/j.1432-1327.1999.00010.x Zobrazit plný text záznamu Plný text ve formátu PDF