FTIR spectroscopy of complexes formed between metarhodopsin II and C‐terminal peptides from the G‐protein α‐ and γ‐subunits

FEBS Letters

Bartl, Franz¹  Ritter, Eglof¹  Hofmann, Klaus Peter¹ 

[1] Institut für Medizinische Physik und Biophysik, Universitätsklinikum Charité, Humboldt Universität zu Berlin, Ziegelstraße 5–9, D-10098 Berlin, Germany

关键词: Rhodopsin;    Fourier transform infrared spectroscopy;    Transducin;    G-protein-coupled receptor;    Signal transduction;    FTIR;    Fourier transform infrared;    MI;    metarhodopsin I;    MII;    metarhodopsin II;    G-protein;    Gt;    heterotrimeric guanine nucleotide binding protein;    Gtα;    Gtγ;    α- and γ-subunits of Gt;   

DOI  :  10.1016/S0014-5793(00)01544-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Metarhodopsin II (MII) provides the active conformation of rhodopsin for interaction with the G-protein, Gt. Fourier transform infrared spectra from samples prepared by centrifugation reflect the pH dependent equilibrium between MII and inactive metarhodopsin I. C-terminal synthetic peptides (Gtα(340–350) and Gtγ(60–71)farnesyl) stabilize MII. We find that both peptides cause similar spectral changes not seen with control peptides (Gtα (K341R, L349A) and non-farnesylated Gtγ). The spectra reflect all the protonation dependent bands normally observed when MII is formed at acidic pH. Beside the protonation dependent bands, additional features, similar with both peptides, appear in the amide I and II regions.

【 授权许可】

Unknown