Structural changes in profilin accompany its binding to phosphatidylinositol 4,5‐bisphosphate

FEBS Letters

Rozycki, Michael¹  Lindberg, Uno³  Mowery, Patrick²  Raghunathan, Vidya¹  Schutt, Clarence¹ 

[1] Frick Chemical Laboratory, Washington Road, Princeton University, Princeton, NJ 08544, USA;American Cyanamid, P.O. Box 400, Princeton NJ 08543-0400, USA;Zoological Cell Biology, WGI, Arrhenius Laboratories for Natural Sciences, Stockholm University, S-10691 Stockholm, Sweden

关键词: Circular dichroism;    Fluorescence;    α-Helix;    Phosphatidylinositol 4;    5-bisphosphate;    Profilin;    Protein conformation;   

DOI  :  10.1016/0014-5793(92)80324-A

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The effect on the structure of profilin of phosphatidylinositol 4,5-bisphosphate (PIP₂) binding was probed by fluorescence and circular dichroism (CD) spectroscopy, Fluorescence of Trp³ and Trp³¹ of profilin at 292 nm showed a linear decrease in solution emission at 340 nm as PIP₂/profilin was increased from 0 to 80:1, apparently due to a static quenching mechanism involving formation of a nonfluorescent PIP₂/profilin complex. CD spectra revealed an increase of up to 3.3-fold in the molar ellipticity at 222 nm for profilin as it binds PIP₂, as well as changes in the Cotton effect between 250 and 310 nm. These results are consistent with a possible increase in the α-helix content or profilin triggered by the binding or PIP₂.

【 授权许可】

Unknown