A short helix in the C-terminal region of LolA is important for the specific membrane localization of lipoproteins

作者：Okuda Suguru; Watanabe Shoji; Tokuda Hajime^*

来源：FEBS Letters, 2008, 582(15): 2247-2251.

DOI：10.1016/j.febslet.2008.05.022

• lipoprotein
• molecular chaperone
• outer membrane
• periplasm
• LolA
• Escherichia coli

The structures of a lipoprotein carrier, LolA, and a lipoprotein receptor, LolB, are similar except for an extra C-terminal loop containing a 3(10) helix and beta-strand 12 in LolA. Lipoprotein release was significantly reduced when beta-12 was deleted. Deletion of the 3(10) helix also inhibited the lipoprotein release. Furthermore, lipoproteins were non-specifically localized to membranes when LolA lacked the 3(10) helix. Thus, the membrane localization of lipoproteins with the LolA derivative lacking the 3(10) helix was independent of LolB whereas LolB was essential for the outer membrane localization of lipoproteins with the wild-type LolA.

• 出版日期2008-6-25