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一种高粱85kDa热应激调节蛋白具有钙调蛋白结合特性，并与抗粗糙脉孢菌热休克蛋白80抗体发生交叉反应。

A sorghum 85kDa heat stress-modulated protein shows calmodulin-binding properties and cross-reactivity to anti-Neurospora crassa Hsp 80 antibodies.

作者信息

Virdi Amardeep Singh, Thakur Aditi, Dutt Som, Kumar Sanjay, Singh Prabhjeet

机构信息

Department of Biotechnology, Guru Nanak Dev University, Amritsar, Punjab 143005, India.

出版信息

FEBS Lett. 2009 Feb 18;583(4):767-70. doi: 10.1016/j.febslet.2009.01.025. Epub 2009 Jan 25.

DOI:10.1016/j.febslet.2009.01.025
PMID:19174162
Abstract

The present study, carried out to identify stress-modulated calmodulin (CaM)-binding proteins in sorghum, resulted in the isolation of several proteins, which showed binding to CaM-Sepharose matrix. Calmodulin gel overlay assay and MALDI-ToF MS analysis revealed that an 85kDa protein (Hsp85), which interacted with calmodulin, cross-reacted with anti-N. crassa Hsp80 antibodies. Since these antibodies bind to plant Hsp90, sorghum Hsp85 is likely to be a member of the Hsp90 family. This study provides the first evidence that a member of Hsp90 (Hsp85) in plants exhibits CaM-binding properties.

摘要

本研究旨在鉴定高粱中受胁迫调节的钙调蛋白（CaM）结合蛋白，结果分离出了几种与CaM-琼脂糖基质结合的蛋白质。钙调蛋白凝胶覆盖分析和基质辅助激光解吸电离飞行时间质谱（MALDI-ToF MS）分析表明，一种与钙调蛋白相互作用的85kDa蛋白质（热休克蛋白85，Hsp85）与抗粗糙脉孢菌热休克蛋白80（Hsp80）抗体发生交叉反应。由于这些抗体与植物热休克蛋白90（Hsp90）结合，高粱Hsp85可能是Hsp90家族的成员。本研究首次提供了植物中Hsp90家族成员（Hsp85）具有CaM结合特性的证据。

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