DISTINCT BIOCHEMICAL CHARACTERISTICS OF THE 2 HUMAN PROFILIN ISOFORMS

被引：52

作者：

GIESELMANN, R

KWIATKOWSKI, DJ

JANMEY, PA

WITKE, W

机构：

[1] HARVARD UNIV, BRIGHAM & WOMENS HOSP,SCH MED,DEPT MED, DIV EXPTL MED, BOSTON, MA 02115 USA

[2] HARVARD UNIV, BRIGHAM & WOMENS HOSP,SCH MED,DEPT MED, DIV HEMATOL ONCOL, BOSTON, MA 02115 USA

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1995年 / 229卷 / 03期

关键词：

HUMAN PROFILIN I; HUMAN PROFILIN II; ACTIN BINDING; NUCLEOTIDE EXCHANGE; PTDINS(4,5)P-2 BINDING;

D O I：

10.1111/j.1432-1033.1995.tb20506.x

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 biochemical characteristics of a new human profilin isoform are described. We refer to this recently described isoform as profilin II (isoelectric point 5.9) in comparison to profilin I (pI 8.4). We expressed both isoforms in bacteria and compared their actin-binding properties, binding to poly(L-proline), affinities for phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P-2], and their effects on nucleotide exchange on actin. Profilin I and profilin II have similar affinities for PtdIns(4,5)P-2 and poly(L-proline), and both accelerate nucleotide exchange on monomeric actin to the same extent. However, the affinity of profilin I for monomeric actin is about five times higher than the affinity of profilin II for actin. Potential structural differences of profilin I and profilin II that might explain the difference in actin binding are discussed.

引用

页码：621 / 628

页数：8

共 47 条

[1] ELUCIDATION OF THE POLY-L-PROLINE BINDING-SITE IN ACANTHAMOEBA PROFILIN-I BY NMR-SPECTROSCOPY [J].