Heat-shock protein 90 (hsp90) binds in vitro to tubulin dimer and inhibits microtubule formation

被引：77

作者：

Garnier, C ^{[1
]}

Barbier, P ^{[1
]}

Gilli, R ^{[1
]}

Lopez, C ^{[1
]}

Peyrot, V ^{[1
]}

Briand, C ^{[1
]}

机构：

[1] Fac Pharm Marseille, CNRS, UPRESA 6032, F-13385 Marseille 5, France

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1998年 / 250卷 / 02期

关键词：

D O I：

10.1006/bbrc.1998.9319

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：

Hsp90 interacts with steroid hormone receptors, protein kinases, and cytoskeletal proteins. The mode of action of hsp90 on microtubules and tubulin has not been investigated. Using isolated purified hsp90 and isolated tubulin, we demonstrated in vitro by difference absorption and fluorescence spectroscopy that hsp90 bound to tubulin with an apparent affinity constant of 5 x 10(5) M-1, assuming an apparent stoichiometry of 1 at 25 degrees C, Using microcalorimetry, we found a Delta H of -9.8 +/- 0.8 kJ.mol(-1). The binding of hsp90 to tubulin was confirmed by a sedimentation assay, Moreover, we showed that hsp90 inhibited tubulin polymerisation. (C) 1998 Academie Press.

引用

页码：414 / 419

页数：6

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