Membrane association of FtsY, the E. coli SRP receptor

FEBS Letters

Poland, Dennis¹  ten Hagen-Jongman, Corinne M¹  Mol, Olaf²  Luirink, Joen¹  Sinning, Irmgard²  de Leeuw, Erik¹  Oudega, Bauke¹ 

[1]Department of Microbiology, Institute of Molecular Biological Sciences, Biocentrum Amsterdam, De Boelelaan 1087, 1081 HV Amsterdam, The Netherlands

[2]European Molecular Biology Laboratory, Structural Biology Programme, Meyerhofstrasse 1, D-69117 Heidelberg, Germany

关键词: Escherichia coli;    FtsY;    Protein targeting;    Signal recognition particle;    ER;    endoplasmic reticulum;    IPTG;    isopropyl-1-thio-β-d-galactopyranoside;    GTP;    guanosine-5′-phosphate;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;    SR;    SRP receptor;    SRP;    signal recognition particle;    WT;    wild-type;   

DOI  :  10.1016/S0014-5793(97)01238-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

FtsY, the Escherichia coli homologue of the eukaryotic SRP receptor (SRα), is located both in the cytoplasm and in the inner membrane of E. coli. Similar to SRα, FtsY consists of two major domains: a strongly acidic N-terminal domain (A) and a C-terminal GTP binding domain (NG) of which the crystal structure has recently been determined. The domains were expressed both in vivo and in vitro to examine their subcellular localization. The results suggest that both domains associate with the membrane but that the nature of the association differs.

【 授权许可】

Unknown