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

Xiaoxi Sun | Zendy; B. Li | Zendy; G.-m. Zhou | Zendy; Wenqiang Tang | Zendy; Jin Bai | Zendy; Daye Sun | Zendy; RenGang Zhou | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

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

Author(s) -

Xiaoxi Sun,

B. Li,

G.-m. Zhou,

Wenqiang Tang,

Jin Bai,

Daye Sun,

RenGang Zhou

Publication year - 2000

Publication title -

plant and cell physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.975

H-Index - 152

eISSN - 1471-9053

pISSN - 0032-0781

DOI - 10.1093/pcp/41.6.804

Subject(s) - calmodulin , hsp70 , cytosol , biotinylation , biochemistry , peptide , peptide sequence , binding site , chemistry , binding protein , biology , heat shock protein , enzyme , gene

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 concentration-dependent 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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research