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

Abstract:

: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 ellpticity 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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Raghunathan V,Mowery P,Rozycki M,Lindberg U,Schutt C

doi

10.1016/0014-5793(92)80324-a

keywords:

subject

Has Abstract

pub_date

1992-02-03 00:00:00

pages

46-50

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(92)80324-A

journal_volume

297

pub_type

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