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

Autor: Stéphane Bourque, David Wendehenne, Jean Borges Bertoldo, Hernán Terenzi, Jeremy Astier, Angélique Besson-Bard, Olivier Lamotte
Přispěvatelé: Agroécologie [Dijon], Institut National de la Recherche Agronomique (INRA)-Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Universidade Federal de Santa Catarina = Federal University of Santa Catarina [Florianópolis] (UFSC), Agence Nationale de la Recherche [BLAN07-2_184783 PIANO], Burgundy State [PARI AGRALE 8], FAPESC (Fundacao de Apoio a Pesquisa Cientifica e Tecnologica do Estado de Santa Catarina), CNPq (Conselho Nacional de Desenvolvimento Cientifico e Tecnologico), MCT/FINEP (Ministerio da Ciencia e Tecnologia/Financiadora de Estudos e Projetos), CAPES (Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior), Ministere Francais de l'Education Nationale, de la Recherche et de la Technologie, Burgundy Sate [FABER project] [PARI AGRALE 8]
Rok vydání: 2012
Předmět:
Zdroj: Biochemical Journal
Biochemical Journal, Portland Press, 2012, 447, pp.249-260. ⟨10.1042/BJ20120257⟩
ISSN: 1470-8728
0264-6021
Popis: NO has important physiological functions in plants, including the adaptative response to pathogen attack. We previously demonstrated that cryptogein, an elicitor of defence reaction produced by the oomycete Phytophthora cryptogea , triggers NO synthesis in tobacco. To decipher the role of NO in tobacco cells elicited by cryptogein, in the present study 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 (cell division cycle 48), a member of the AAA+ ATPase (ATPase associated with various cellular activities) family. In vitro , NtCDC48 ( Nicotiana tabacum CDC48) 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, that is 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 alanine residue had an impact on NtCDC48 activity. More generally, the present 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.
Databáze: OpenAIRE