Dominant negative mutant of a lipoprotein‐specific molecular chaperone, LolA, tightly associates with LolCDE

FEBS Letters

Matsuyama, Shin-ichi¹  Tokuda, Hajime¹  Miyamoto, Atsuki¹ 

[1]Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan

关键词: Lipoprotein;    Molecular chaperone;    Membrane anchoring;    Proteoliposome;    ATP binding cassette transporter;    Periplasm;    ABC;    ATP binding cassette;    LolCDE;    a complex containing one molecule each of LolC and LolE;    and two molecules of LolD;    LolA;    a periplasmic molecular chaperone for lipoproteins;    LolB;    lipoprotein receptor in the outer membrane;    MalFGK2;    a complex containing one molecule each of MalF and MalG;    and two molecules of MalK;   

DOI  :  10.1016/S0014-5793(02)03305-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Periplasmic molecular chaperone LolA and the inner membrane ATP binding cassette transporter LolCDE are essential for ATP-dependent release of outer membrane-directed lipoproteins from the inner membrane of Escherichia coli. A LolA(F47E) mutant carrying a Phe to Glu mutation at position 47 was defective in the release of lipoproteins from spheroplasts and proteoliposomes reconstituted with LolCDE. When incubated with proteoliposomes containing LolCDE, LolA remained in the supernatant whereas LolA(F47E) bound to proteoliposomes. This tight association of LolA(F47E) with LolCDE caused a dominant negative phenotype in vivo, suggesting that the LolA–LolCDE interaction is critical for lipoprotein release.

【 授权许可】

Unknown