Journal Article

Binding of the Maize Cytosolic Hsp70 to Calmodulin, and Identification of Calmodulin-Binding Site in Hsp70

Xu-tong Sun, Bing Li, Gou-min Zhou, Wen-qiang Tang, Juan Bai, Da-ye Sun and Ren-gang Zhou

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 41, issue 6, pages 804-810
Published in print June 2000 | ISSN: 0032-0781
Published online June 2000 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/41.6.804
Binding of the Maize Cytosolic Hsp70 to Calmodulin, and Identification of Calmodulin-Binding Site in Hsp70

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Using a gel-overlay technique of biotinylated calmodulin (CaM), we showed that maize cytosolic Hsp70 protein could bind to CaM in the presence of 1 mM CaCl2. The purified maize cytosolic Hsp70 inhibited the activity of CaM-dependent NADK in a concentrationdependent manner. A synthetic peptide, which possesses the 21 amino acid sequence, PRALRRLRTACERAKRTLSST, at positions 261–281 in maize cytosolic Hsp70, could associate with CaM in the presence of 1 mM calcium. The synthetic peptide inhibited CaM-dependent NADK activity and PDE activity. This indicates that the 21-amino acid sequence at positions 261–281 is the CaM-binding site. The binding of CaM to Hsp70 inhibited the ATPase activity of Hsp70. The possible regulator function of Hsp70 in cell signaling events in response to heat stress is discussed.

Keywords: Calmodulin-binding protein; Hsp70; Signal transduction

Journal Article.  0 words. 

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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