Nitric oxide inhibits the ATPase activity of the chaperone-like AAA+ATPase CDC48, a target for S-nitrosylation in cryptogein signaling in tobacco cells.

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Nitric oxide inhibits the ATPase activity of the chaperone-like AAA+ATPase CDC48, a target for S-nitrosylation in cryptogein signaling in tobacco cells.

Biochem J. 2012 Jul 27;

Authors: Astier J, Besson-Bard A, Lamotte O, Bertoldo J, Bourque S, Terenzi H, Wendehenne D

Abstract
Nitric oxide (NO) has important physiological functions in plants including the adaptative response to pathogen attack. We previously demonstrated that cryptogein, an elicitor of defense reaction produced by the oomycete Phytophthora cryptogea, triggers NO synthesis in tobacco. To decipher the role of NO in tobacco cells elicited by cryptogein, here we performed a proteomic approach in order to identify proteins undergoing S-nitrosylation. We provided evidence that cryptogein induced the S-nitrosylation of several proteins and identified 11 candidates including CDC48, a member of the AAA+ATPases. In vitro, NtCDC48 was shown to be poly-S-nitrosylated by NO donors and we could identify Cys-110, Cys-526 and Cys-664 as a targets for S-nitrosylation. Cys-526 is located in the Walker A motif of the D2 domain involved in ATP binding and was previously reported to be regulated by oxidative modification in drosophila. We investigated the consequence of NtCDC48 S-nitrosylation and found that NO abolished NtCDC48 ATPase activity and induced slight conformation changes in the vicinity of Cys-526. Similarly, substitution of Cys-526 by an Ala residue impacted NtCDC48 activity. More generally, our study identified CDC48 as a new candidate for S-nitrosylation in plants facing biotic stress and further supports the importance of Cys-526 in the regulation of CDC48 by oxidative/nitrosative agents.

PMID: 22835150 [PubMed - as supplied by publisher]

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