Cloning and characterization of actin depolymerizing factor from Toxoplasma gondii

被引：62

作者：

Allen, ML

Dobrowolski, JM

Muller, H

Sibley, LD

Mansour, TE

机构：

[1] STANFORD UNIV,SCH MED,DEPT MOL PHARMACOL,STANFORD,CA 94305

[2] WASHINGTON UNIV,SCH MED,DEPT MOL MICROBIOL,ST LOUIS,MO 63110

来源：

MOLECULAR AND BIOCHEMICAL PARASITOLOGY | 1997年 / 88卷 / 1-2期

关键词：

Toxoplasma gondii; actin depolymerizing factor; cytoskeleton;

D O I：

10.1016/S0166-6851(97)00069-8

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：

We determined the predicted amino acid sequence of actin depolymerizing factor (ADF) from Taxoplasma gondii by sequencing the full-length cDNA. T. gondii ADF consists of 118 amino acids (calculated molecular weight 13400) and shares a high degree of sequence similarity to other low molecular weight actin monomer sequestering proteins, especially Acanthamoeba actophorin, plant ADFs and yeast and vertebrate cofilin. ADF from T. gondii is smaller and does not contain a nuclear localization sequence like the related vertebrate proteins. Southern blot analysis indicates that T. gondii ADF is a single-copy gene. Homogeneous recombinant T. gondii ADF purified from E. coli is active in binding actin monomers and depolymerizing F-actin. Localization of ADF by immunofluorescence and immuno-electron microscopy indicates ADF is scattered throughout the cytoplasm and prominently localized beneath the plasma membrane in T. gondii. (C) 1997 Elsevier Science B.V.

引用

页码：43 / 52

页数：10

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