The conformational bases for the two functionalities of 2-cysteine peroxiredoxins as peroxidase and chaperone

König J, Galliardt H, Jütte P, Schäper S, Dittmann L, Dietz K-J (2013)
Journal of experimental botany 64(11): 3483-3497.

Zeitschriftenaufsatz | Veröffentlicht| Englisch
 
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Autor/in
König, JanineUniBi; Galliardt, HelenaUniBi; Jütte, Patrick; Schäper, Simon; Dittmann, Lea; Dietz, Karl-JosefUniBi
Abstract / Bemerkung
2-Cysteine peroxiredoxins (2-CysPrxs) are ubiquitous and highly abundant proteins that serve multiple functions as peroxidases, chaperones, and thiol oxidases and in redox-dependent cell signalling. The chloroplast protein plays a role in seedling development and protection of the photosynthetic apparatus. This study aimed to unequivocally link conformation and function. To this end, a set of non-tagged site-directed mutagenized At2-CysPrx variants was engineered, which mimicked the conformational states and their specific functions: hyperoxidized form (C54D), reduced form (C54S, C176S), oxidized form (C54DC176K), phosphorylated form (T92D), reduced ability for oligomerization by interfering with the dimer-dimer interface (F84R) and a C-terminally truncated form [ΔC (-20 aa)]. These variants were fully or partly fixed in their quaternary structure and function, respectively, and were analysed for their conformational state and peroxidase and chaperone activity, as well as for their sensitivity to hyperoxidation. The presence of a His6-tag strongly influenced the properties of the protein. The ΔC variant became insensitive to hyperoxidation, while T92D and F84R became more sensitive. The C54D variant revealed the highest chaperone activity. The highest peroxidase activity was observed for the F84R and ΔC variants. Efficient interaction with NADP-dependent thioredoxin reductase C depended on the presence of Cys residues and the C-terminal tail. The results suggest that the structural flexibility is important for the switch between peroxidase and chaperone function and that evolution has conserved the functional switch instead of maximizing a single function. These variants are ideal tools for future conformation-specific studies in vivo and in vitro.
Erscheinungsjahr
2013
Zeitschriftentitel
Journal of experimental botany
Band
64
Ausgabe
11
Seite(n)
3483-3497
ISSN
0022-0957
eISSN
1460-2431
Page URI
https://pub.uni-bielefeld.de/record/2621205

Zitieren

König J, Galliardt H, Jütte P, Schäper S, Dittmann L, Dietz K-J. The conformational bases for the two functionalities of 2-cysteine peroxiredoxins as peroxidase and chaperone. Journal of experimental botany. 2013;64(11):3483-3497.
König, J., Galliardt, H., Jütte, P., Schäper, S., Dittmann, L., & Dietz, K. - J. (2013). The conformational bases for the two functionalities of 2-cysteine peroxiredoxins as peroxidase and chaperone. Journal of experimental botany, 64(11), 3483-3497. doi:10.1093/jxb/ert184
König, J., Galliardt, H., Jütte, P., Schäper, S., Dittmann, L., and Dietz, K. - J. (2013). The conformational bases for the two functionalities of 2-cysteine peroxiredoxins as peroxidase and chaperone. Journal of experimental botany 64, 3483-3497.
König, J., et al., 2013. The conformational bases for the two functionalities of 2-cysteine peroxiredoxins as peroxidase and chaperone. Journal of experimental botany, 64(11), p 3483-3497.
J. König, et al., “The conformational bases for the two functionalities of 2-cysteine peroxiredoxins as peroxidase and chaperone”, Journal of experimental botany, vol. 64, 2013, pp. 3483-3497.
König, J., Galliardt, H., Jütte, P., Schäper, S., Dittmann, L., Dietz, K.-J.: The conformational bases for the two functionalities of 2-cysteine peroxiredoxins as peroxidase and chaperone. Journal of experimental botany. 64, 3483-3497 (2013).
König, Janine, Galliardt, Helena, Jütte, Patrick, Schäper, Simon, Dittmann, Lea, and Dietz, Karl-Josef. “The conformational bases for the two functionalities of 2-cysteine peroxiredoxins as peroxidase and chaperone”. Journal of experimental botany 64.11 (2013): 3483-3497.

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