Journal
BIOCHEMICAL JOURNAL
Volume 383, Issue -, Pages 73-81Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20031907
Keywords
Arabidopsis thaliana; autophosphorylation; calmodulin; capillary electrophoresis; Ca2+-dependent protein-kinase (CDPK)-related protein kinase (CRK)
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An AtCRK1 [Arabidopsis thaliana CDPK (Ca2+-dependent protein kinase)-related protein kinase 1] has been characterized molecularly and biochemically. AtCRK1 contains the kinase catalytic domain and a CaM (calmodulin)-binding site. Our results demonstrated that AtCRK1 could bind CaM in a Ca2+-dependent manner. This kinase phosphorylated itself and substrates such as histone HIS and syntide-2 in a Ca2+-independent manner and the activity was stimulated by several CaM isoforms through its CaN-binding domain. This domain was localized within a stretch of 39 amino acid residues at positions from 403 to 441 with K-d = 67 nM for CaM binding. However, the stimulation amplification of the kinase activity of AtCRK1 by different CaM isoforms was similar.
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