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Ca2+-dependent interaction between calmodulin and CoDN3, an effector of Colletotrichum orbiculare

Ca2+-dependent interaction between calmodulin and CoDN3, an effector of Colletotrichum orbiculare

Biochemical and Biophysical Research Communications 514(3): 803-808

ISSN/ISBN: 0006-291X

PMID: 31079920

DOI: 10.1016/j.bbrc.2019.05.007

Nuclear magnetic resonance (NMR) data directly indicated a Ca2+-dependent interaction between calmodulin (CaM) and CoDN3, a small effector of the plant pathogenic fungus Colletotrichum orbiculare, which is the causal agent of cucumber anthracnose. The overall conformation of CoDN3 is intrinsically disordered, and the CaM-binding site spans residues 34-53 of its C-terminal region. Experiments employing a chemically synthesized peptide corresponding to the CaM-binding site indicated that the CaM-binding region of CoDN3 in the Ca2+-bound CaM complex takes an α-helical conformation. Cell death suppression assay using a CoDN3 mutant lacking the CaM-binding ability suggested that the wild type CaM-binding site is necessary for full CoDN3 function in vivo.

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Accession: 066776097

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