Functional heterogeneity of transducin α subunits

FEBS Letters

Neubert, Thomas A¹  Hurley, James B¹ 

[1] Department of Biochemistry and Howard Hughes Medical Institute, University of Washington School of Medicine, Box 357370, Seattle, WA 98195, USA

关键词: Transducin;    Phototransduction;    Myristoylation;    G-protein;    Mass spectrometry;    Tr;    rod transducin;    Tαβγ;    the α;    β and γ subunits of transducin;    PDE;    cyclic GMP phosphodiesterase;    ROS;    rod outer segments;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;    HPLC;    high performance liquid chromatography;    ESI-MS;    electrospray ionization mass spectrometry;    TFA;    trifluoroacetic acid;   

DOI  :  10.1016/S0014-5793(98)00037-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The N-terminal glycine of transducin α subunits is acylated by lauroyl (C12:0), myristoyl (C14:0), (cis-Δ⁵)-tetradecaenoyl (C14:1) or (cis,cis-Δ⁵,Δ⁸)-tetradecadienoyl (C14:2) fatty acyl groups. We examined functional heterogeneity of transducin by sequentially eluting it from bleached outer segments using increasing concentrations of GTP then identifying the N-terminal acyl groups on the eluted α subunits. C14:2 acylated transducin eluted at low GTP concentrations followed by C12:0, C14:1 and C14:0 transducin at higher GTP concentrations. This suggests functional heterogeneity in the different forms of transducin α subunits.

【 授权许可】

Unknown