STRUCTURAL-CHANGES IN PROFILIN ACCOMPANY ITS BINDING TO PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE

被引：45

作者：

RAGHUNATHAN, V

MOWERY, P

ROZYCKI, M

LINDBERG, U

SCHUTT, C

机构：

[1] PRINCETON UNIV,FRICK CHEM LAB,WASHINGTON RD,PRINCETON,NJ 08544

[2] AMER CYANAMID CO,PRINCETON,NJ 08543

[3] UNIV STOCKHOLM,ARRHENIUS LABS NAT SCI,WGI,S-10691 STOCKHOLM,SWEDEN

来源：

FEBS LETTERS | 1992年 / 297卷 / 1-2期

关键词：

CIRCULAR DICHROISM; FLUORESCENCE; ALPHA-HELIX; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE; PROFILIN; PROTEIN CONFORMATION;

D O I：

10.1016/0014-5793(92)80324-A

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 alpha-helix content of profilin triggered by the binding of PIP2.

引用

页码：46 / 50

页数：5

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