The oligomeric conformation of peroxiredoxins links redox state to function
Barranco-Medina S, Lazaro J-J, Dietz K-J (2009)
FEBS LETTERS 583(12): 1809-1816.
Zeitschriftenaufsatz
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Autor*in
Barranco-Medina, Sergio;
Lazaro, Juan-Jose;
Dietz, Karl-JosefUniBi
Einrichtung
Abstract / Bemerkung
Protein-protein associations, i.e. formation of permanent or transient protein complexes, are essential for protein functionality and regulation within the cellular context. Peroxiredoxins (Prx) undergo major redox-dependent conformational changes and the dynamics are linked to functional switches. While a large number of investigations have addressed the principles and functions of Prx oligomerization, understanding of the diverse in vivo roles of this conserved redox-dependent feature of Prx is slowly emerging. The review summarizes studies on Prx oligomerization, its tight connection to the redox state, and the knowledge and hypotheses on its physiological function in the cell as peroxidase, chaperone, binding partner, enzyme activator and/or redox sensor. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Stichworte
Protein oligomerization;
Sulfiredoxin;
Chaperone;
activity;
Dithiothreitol;
Peroxiredoxin
Erscheinungsjahr
2009
Zeitschriftentitel
FEBS LETTERS
Band
583
Ausgabe
12
Seite(n)
1809-1816
ISSN
0014-5793
Page URI
https://pub.uni-bielefeld.de/record/1591737
Zitieren
Barranco-Medina S, Lazaro J-J, Dietz K-J. The oligomeric conformation of peroxiredoxins links redox state to function. FEBS LETTERS. 2009;583(12):1809-1816.
Barranco-Medina, S., Lazaro, J. - J., & Dietz, K. - J. (2009). The oligomeric conformation of peroxiredoxins links redox state to function. FEBS LETTERS, 583(12), 1809-1816. https://doi.org/10.1016/j.febslet.2009.05.029
Barranco-Medina, Sergio, Lazaro, Juan-Jose, and Dietz, Karl-Josef. 2009. “The oligomeric conformation of peroxiredoxins links redox state to function”. FEBS LETTERS 583 (12): 1809-1816.
Barranco-Medina, S., Lazaro, J. - J., and Dietz, K. - J. (2009). The oligomeric conformation of peroxiredoxins links redox state to function. FEBS LETTERS 583, 1809-1816.
Barranco-Medina, S., Lazaro, J.-J., & Dietz, K.-J., 2009. The oligomeric conformation of peroxiredoxins links redox state to function. FEBS LETTERS, 583(12), p 1809-1816.
S. Barranco-Medina, J.-J. Lazaro, and K.-J. Dietz, “The oligomeric conformation of peroxiredoxins links redox state to function”, FEBS LETTERS, vol. 583, 2009, pp. 1809-1816.
Barranco-Medina, S., Lazaro, J.-J., Dietz, K.-J.: The oligomeric conformation of peroxiredoxins links redox state to function. FEBS LETTERS. 583, 1809-1816 (2009).
Barranco-Medina, Sergio, Lazaro, Juan-Jose, and Dietz, Karl-Josef. “The oligomeric conformation of peroxiredoxins links redox state to function”. FEBS LETTERS 583.12 (2009): 1809-1816.
Daten bereitgestellt von European Bioinformatics Institute (EBI)
96 Zitationen in Europe PMC
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Lee W, Choi KS, Riddell J, Ip C, Ghosh D, Park JH, Park YM., J. Biol. Chem. 282(30), 2007
PMID: 17519234
Lee W, Choi KS, Riddell J, Ip C, Ghosh D, Park JH, Park YM., J. Biol. Chem. 282(30), 2007
PMID: 17519234
Dimer-oligomer interconversion of wild-type and mutant rat 2-Cys peroxiredoxin: disulfide formation at dimer-dimer interfaces is not essential for decamerization.
Matsumura T, Okamoto K, Iwahara S, Hori H, Takahashi Y, Nishino T, Abe Y., J. Biol. Chem. 283(1), 2007
PMID: 17974571
Matsumura T, Okamoto K, Iwahara S, Hori H, Takahashi Y, Nishino T, Abe Y., J. Biol. Chem. 283(1), 2007
PMID: 17974571
Oligomeric Hsp33 with enhanced chaperone activity: gel filtration, cross-linking, and small angle x-ray scattering (SAXS) analysis.
Akhtar MW, Srinivas V, Raman B, Ramakrishna T, Inobe T, Maki K, Arai M, Kuwajima K, Rao ChM., J. Biol. Chem. 279(53), 2004
PMID: 15494414
Akhtar MW, Srinivas V, Raman B, Ramakrishna T, Inobe T, Maki K, Arai M, Kuwajima K, Rao ChM., J. Biol. Chem. 279(53), 2004
PMID: 15494414
Regulation of peroxiredoxin expression versus expression of Halliwell-Asada-Cycle enzymes during early seedling development of Arabidopsis thaliana.
Pena-Ahumada A, Kahmann U, Dietz KJ, Baier M., Photosyn. Res. 89(2-3), 2006
PMID: 16915352
Pena-Ahumada A, Kahmann U, Dietz KJ, Baier M., Photosyn. Res. 89(2-3), 2006
PMID: 16915352
Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases.
Baier M, Dietz KJ., Plant Mol. Biol. 31(3), 1996
PMID: 8790288
Baier M, Dietz KJ., Plant Mol. Biol. 31(3), 1996
PMID: 8790288
Protective function of chloroplast 2-cysteine peroxiredoxin in photosynthesis. Evidence from transgenic Arabidopsis.
Baier M, Dietz KJ., Plant Physiol. 119(4), 1999
PMID: 10198100
Baier M, Dietz KJ., Plant Physiol. 119(4), 1999
PMID: 10198100
Non-reductive modulation of chloroplast fructose-1,6-bisphosphatase by 2-Cys peroxiredoxin.
Caporaletti D, D'Alessio AC, Rodriguez-Suarez RJ, Senn AM, Duek PD, Wolosiuk RA., Biochem. Biophys. Res. Commun. 355(3), 2007
PMID: 17307139
Caporaletti D, D'Alessio AC, Rodriguez-Suarez RJ, Senn AM, Duek PD, Wolosiuk RA., Biochem. Biophys. Res. Commun. 355(3), 2007
PMID: 17307139
ATP-dependent modulation and autophosphorylation of rapeseed 2-Cys peroxiredoxin
Aran, FEBS Lett. 275(), 2007
Aran, FEBS Lett. 275(), 2007
Crystal structure of a dimeric oxidized form of human peroxiredoxin 5.
Evrard C, Capron A, Marchand C, Clippe A, Wattiez R, Soumillion P, Knoops B, Declercq JP., J. Mol. Biol. 337(5), 2004
PMID: 15046979
Evrard C, Capron A, Marchand C, Clippe A, Wattiez R, Soumillion P, Knoops B, Declercq JP., J. Mol. Biol. 337(5), 2004
PMID: 15046979
The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins.
Smeets A, Marchand C, Linard D, Knoops B, Declercq JP., Arch. Biochem. Biophys. 477(1), 2008
PMID: 18489898
Smeets A, Marchand C, Linard D, Knoops B, Declercq JP., Arch. Biochem. Biophys. 477(1), 2008
PMID: 18489898
Hexameric oligomerization of mitochondrial peroxiredoxin PrxIIF and formation of an ultrahigh affinity complex with its electron donor thioredoxin Trx-o.
Barranco-Medina S, Krell T, Bernier-Villamor L, Sevilla F, Lazaro JJ, Dietz KJ., J. Exp. Bot. 59(12), 2008
PMID: 18632730
Barranco-Medina S, Krell T, Bernier-Villamor L, Sevilla F, Lazaro JJ, Dietz KJ., J. Exp. Bot. 59(12), 2008
PMID: 18632730
Cloning, overexpression, purification and preliminary crystallographic studies of a mitochondrial type II peroxiredoxin from Pisum sativum.
Barranco-Medina S, Lopez-Jaramillo FJ, Bernier-Villamor L, Sevilla F, Lazaro JJ., Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62(Pt 7), 2006
PMID: 16820697
Barranco-Medina S, Lopez-Jaramillo FJ, Bernier-Villamor L, Sevilla F, Lazaro JJ., Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62(Pt 7), 2006
PMID: 16820697
The tetrameric structure of Haemophilus influenza hybrid Prx5 reveals interactions between electron donor and acceptor proteins.
Kim SJ, Woo JR, Hwang YS, Jeong DG, Shin DH, Kim K, Ryu SE., J. Biol. Chem. 278(12), 2003
PMID: 12529327
Kim SJ, Woo JR, Hwang YS, Jeong DG, Shin DH, Kim K, Ryu SE., J. Biol. Chem. 278(12), 2003
PMID: 12529327
Catalytic mechanism of thiol peroxidase from Escherichia coli. Sulfenic acid formation and overoxidation of essential CYS61.
Baker LM, Poole LB., J. Biol. Chem. 278(11), 2003
PMID: 12514184
Baker LM, Poole LB., J. Biol. Chem. 278(11), 2003
PMID: 12514184
Crystal structure of Escherichia coli thiol peroxidase in the oxidized state: insights into intramolecular disulfide formation and substrate binding in atypical 2-Cys peroxiredoxins.
Choi J, Choi S, Choi J, Cha MK, Kim IH, Shin W., J. Biol. Chem. 278(49), 2003
PMID: 14506251
Choi J, Choi S, Choi J, Cha MK, Kim IH, Shin W., J. Biol. Chem. 278(49), 2003
PMID: 14506251
Reversible conformational switch revealed by the redox structures of Bacillus subtilis thiol peroxidase.
Lu J, Yang F, Li Y, Zhang X, Xia B, Jin C., Biochem. Biophys. Res. Commun. 373(3), 2008
PMID: 18588855
Lu J, Yang F, Li Y, Zhang X, Xia B, Jin C., Biochem. Biophys. Res. Commun. 373(3), 2008
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Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution.
Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE., Nat. Struct. Biol. 5(5), 1998
PMID: 9587003
Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE., Nat. Struct. Biol. 5(5), 1998
PMID: 9587003
Interaction of surfactant protein A with peroxiredoxin 6 regulates phospholipase A2 activity.
Wu YZ, Manevich Y, Baldwin JL, Dodia C, Yu K, Feinstein SI, Fisher AB., J. Biol. Chem. 281(11), 2005
PMID: 16330552
Wu YZ, Manevich Y, Baldwin JL, Dodia C, Yu K, Feinstein SI, Fisher AB., J. Biol. Chem. 281(11), 2005
PMID: 16330552
Biochemical characterization of Toxoplasma gondii 1-Cys peroxiredoxin 2 with mechanistic similarities to typical 2-Cys Prx.
Deponte M, Becker K., Mol. Biochem. Parasitol. 140(1), 2005
PMID: 15694490
Deponte M, Becker K., Mol. Biochem. Parasitol. 140(1), 2005
PMID: 15694490
Characterization of novel hexadecameric thioredoxin peroxidase from Aeropyrum pernix K1.
Jeon SJ, Ishikawa K., J. Biol. Chem. 278(26), 2003
PMID: 12707274
Jeon SJ, Ishikawa K., J. Biol. Chem. 278(26), 2003
PMID: 12707274
Crystal structure of an archaeal peroxiredoxin from the aerobic hyperthermophilic crenarchaeon Aeropyrum pernix K1.
Mizohata E, Sakai H, Fusatomi E, Terada T, Murayama K, Shirouzu M, Yokoyama S., J. Mol. Biol. 354(2), 2005
PMID: 16214169
Mizohata E, Sakai H, Fusatomi E, Terada T, Murayama K, Shirouzu M, Yokoyama S., J. Mol. Biol. 354(2), 2005
PMID: 16214169
The crystal structure of the C45S mutant of annelid Arenicola marina peroxiredoxin 6 supports its assignment to the mechanistically typical 2-Cys subfamily without any formation of toroid-shaped decamers.
Smeets A, Loumaye E, Clippe A, Rees JF, Knoops B, Declercq JP., Protein Sci. 17(4), 2008
PMID: 18359859
Smeets A, Loumaye E, Clippe A, Rees JF, Knoops B, Declercq JP., Protein Sci. 17(4), 2008
PMID: 18359859
Study of the quarternary structure of rat 1-Cys peroxiredoxin
Bystrova, Biofzika 52(), 2007
Bystrova, Biofzika 52(), 2007
Crystal Structure of AhpE from Mycobacterium tuberculosis, a 1-Cys peroxiredoxin.
Li S, Peterson NA, Kim MY, Kim CY, Hung LW, Yu M, Lekin T, Segelke BW, Lott JS, Baker EN., J. Mol. Biol. 346(4), 2005
PMID: 15701515
Li S, Peterson NA, Kim MY, Kim CY, Hung LW, Yu M, Lekin T, Segelke BW, Lott JS, Baker EN., J. Mol. Biol. 346(4), 2005
PMID: 15701515
Glutathionylation induces the dissociation of 1-Cys D-peroxiredoxin non-covalent homodimer.
Noguera-Mazon V, Lemoine J, Walker O, Rouhier N, Salvador A, Jacquot JP, Lancelin JM, Krimm I., J. Biol. Chem. 281(42), 2006
PMID: 16916801
Noguera-Mazon V, Lemoine J, Walker O, Rouhier N, Salvador A, Jacquot JP, Lancelin JM, Krimm I., J. Biol. Chem. 281(42), 2006
PMID: 16916801
Characterization of the complex of glutathione S-transferase pi and 1-cysteine peroxiredoxin.
Ralat LA, Misquitta SA, Manevich Y, Fisher AB, Colman RF., Arch. Biochem. Biophys. 474(1), 2008
PMID: 18358825
Ralat LA, Misquitta SA, Manevich Y, Fisher AB, Colman RF., Arch. Biochem. Biophys. 474(1), 2008
PMID: 18358825
Reduction of 1-Cys peroxiredoxins by ascorbate changes the thiol-specific antioxidant paradigm, revealing another function of vitamin C.
Monteiro G, Horta BB, Pimenta DC, Augusto O, Netto LE., Proc. Natl. Acad. Sci. U.S.A. 104(12), 2007
PMID: 17360337
Monteiro G, Horta BB, Pimenta DC, Augusto O, Netto LE., Proc. Natl. Acad. Sci. U.S.A. 104(12), 2007
PMID: 17360337
Biomimetic magnetic nanoparticles
Klem, Mater. Today (), 2005
Klem, Mater. Today (), 2005
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