Interaction of ADP-ribosylated actin with actin binding proteins

被引：18

作者：

Ballweber, E

Galla, M

Aktories, K

Yeoh, S

Weeds, AG

Mannherz, HG

机构：

[1] Ruhr Univ Bochum, Dept Anat & Cell Biol, D-44780 Bochum, Germany

[2] Univ Freiburg, Inst Expt & Clin Pharmacol & Toxicol, Freiburg, Germany

[3] MRC, Mol Biol Lab, Cambridge CB2 2QH, England

来源：

FEBS LETTERS | 2001年 / 508卷 / 01期

关键词：

actin binding protein; ADP-ribosylated actin;

D O I：

10.1016/S0014-5793(01)03040-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：

Actin ADP-ribosylated at Arg177 was previously shown not to polymerise after increasing the ionic strength, but to cap the barbed ends of filaments. Here we confirm that the polymerisation of ADP-ribosylated actin is inhibited, however, under specific conditions the modified actin copolymerises with native actin, indicating that its ability to take part in normal subunit interactions within filaments is not fully eliminated. We also show that ADP-ribosylated actin forms antiparallel but not parallel dimers: the former are not able to form filaments. ADP-ribosylated actin interacts with deoxyribonuclease 1, vitamin D binding protein, thymosin beta (4), cofilin and gelsolin segment I like native actin. Interaction with myosin subfragment I revealed that the potential of the modified actin to aggregate into oligomers or short filaments is not fully eliminated. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

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收藏

页码：131 / 135

页数：5

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