Role of the cysteine residues in Arabidopsis thaliana cyclophilin CYP20-3 in peptidyl-prolyl cis-trans isomerase and redox-related functions

Laxa M, König J, Dietz K-J, Kandlbinder A (2007)
BIOCHEMICAL JOURNAL 401(1): 287-297.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Abstract / Bemerkung
Cyps (cyclophilins) are ubiquitous proteins of the immunophilin superfamily with proposed functions in protein folding, protein degradation, stress response and signal transduction. Conserved cysteine residues further suggest a roll in redox regulation. In order to get insight into the conformational change mechanism and functional properties of the chloroplast-located CYP20-3, site-directed mutagenized cysteine -> serine variants were generated and analysed for enzymatic and conformational properties under reducing and oxidizing conditions. Compared with the wildtype form, elimination of three out of the four cysteine residues decreased the catalytic efficiency of PIPI (peptidyi-prolyl cis-trans isomerase) activity of the reduced CYP20-3, indicating a regulatory role of dithiol-disulfide transitions in protein function. Oxidation was accompanied by conformational changes with a predominant role in the structural rearrangement of the disulfide bridge formed between Cys(54) and Cys(171). The rather negative E-m (midpoint redox potential) of -319 mV places CYP20-3 into the redox hierarchy of the chloroplast, suggesting the activation of CYP20-3 in the light under conditions of limited acceptor availability for photosynthesis as realized under environmental stress. Chloroplast Prx (peroxiredoxins) were identified as interacting partners of CYP20-3 in a DNA-protection assay. A catalytic role in the reduction of 2-Cys PrxA and 2-Cys PrxB was assigned to Cys(129) and Cys(171). In addition, it was shown that the isomerization and disulfide-reduction activities are two independent functions of CYP20-3 that both are regulated by the redox state of its active centre.
Stichworte
chloroplast; peroxiredoxin; immunophilin; peptidyl-prolyl cis-trans isomerase (PPI); cyclophilin; Arabidopsis thaliana
Erscheinungsjahr
2007
Zeitschriftentitel
BIOCHEMICAL JOURNAL
Band
401
Ausgabe
1
Seite(n)
287-297
ISSN
0264-6021
eISSN
1470-8728
Page URI
https://pub.uni-bielefeld.de/record/1596187

Zitieren

Laxa M, König J, Dietz K-J, Kandlbinder A. Role of the cysteine residues in Arabidopsis thaliana cyclophilin CYP20-3 in peptidyl-prolyl cis-trans isomerase and redox-related functions. BIOCHEMICAL JOURNAL. 2007;401(1):287-297.
Laxa, M., König, J., Dietz, K. - J., & Kandlbinder, A. (2007). Role of the cysteine residues in Arabidopsis thaliana cyclophilin CYP20-3 in peptidyl-prolyl cis-trans isomerase and redox-related functions. BIOCHEMICAL JOURNAL, 401(1), 287-297. doi:10.1042/BJ20061092
Laxa, M., König, J., Dietz, K. - J., and Kandlbinder, A. (2007). Role of the cysteine residues in Arabidopsis thaliana cyclophilin CYP20-3 in peptidyl-prolyl cis-trans isomerase and redox-related functions. BIOCHEMICAL JOURNAL 401, 287-297.
Laxa, M., et al., 2007. Role of the cysteine residues in Arabidopsis thaliana cyclophilin CYP20-3 in peptidyl-prolyl cis-trans isomerase and redox-related functions. BIOCHEMICAL JOURNAL, 401(1), p 287-297.
M. Laxa, et al., “Role of the cysteine residues in Arabidopsis thaliana cyclophilin CYP20-3 in peptidyl-prolyl cis-trans isomerase and redox-related functions”, BIOCHEMICAL JOURNAL, vol. 401, 2007, pp. 287-297.
Laxa, M., König, J., Dietz, K.-J., Kandlbinder, A.: Role of the cysteine residues in Arabidopsis thaliana cyclophilin CYP20-3 in peptidyl-prolyl cis-trans isomerase and redox-related functions. BIOCHEMICAL JOURNAL. 401, 287-297 (2007).
Laxa, Miriam, König, Janine, Dietz, Karl-Josef, and Kandlbinder, Andrea. “Role of the cysteine residues in Arabidopsis thaliana cyclophilin CYP20-3 in peptidyl-prolyl cis-trans isomerase and redox-related functions”. BIOCHEMICAL JOURNAL 401.1 (2007): 287-297.

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