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

Abstract：

: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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Isozumi N,Inoue Y,Imamura T,Mori M,Takano Y,Ohki S

doi

10.1016/j.bbrc.2019.05.007

subject

Has Abstract

pub_date

2019-06-30 00:00:00

pages

803-808

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(19)30875-7

journal_volume

514

pub_type

杂志文章

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