The involvement of the mitochondrial peroxiredoxin PRXIIF in defining physiological differences between orthodox and recalcitrant seeds of two Acer species
Ewelina Ratajczak A B C , Elke Ströher B , Marie-Luise Oelze B , Ewa M. Kalemba A , Stanisława Pukacka A and Karl-Josef Dietz B
+ Author Affiliations
- Author Affiliations
A Institute of Dendrology, Polish Academy of Sciences, Seed Biochemistry Laboratory, Parkowa 5, 62-035 Kórnik, Poland.
B Department of Biochemistry and Physiology of Plants, Bielefeld University, University Street 25, Bielefeld 33501, Germany.
C Corresponding author. Email: eratajcz@man.poznan.pl
Functional Plant Biology 40(10) 1005-1017 https://doi.org/10.1071/FP13002
Submitted: 2 January 2013 Accepted: 27 March 2013 Published: 3 June 2013
Abstract
Norway maple (Acer platanoides L., orthodox) and sycamore (Acer pseudoplatanus L., recalcitrant) belong to the same genus and grow under similar climatic conditions, but their seeds differ in their tolerance to desiccation. The initial water content (WC) of the seeds used in this study was 50%, and they were dried to 40, 20 and 7%. The mitochondrial peroxiredoxin IIF (PRXIIF) was identified in seeds of both species by immunoblotting. Semiquantitative RT–PCR analyses indicated that the transcript level of PRXIIF in both types of seeds increased during different stages of desiccation and was higher in seeds of Norway maple than in sycamore. General proteome analyses showed important differences between orthodox and recalcitrant seeds. In sycamore seeds that had been desiccated to a 7% WC, the number of protein spots and the levels of those spots were lower than in desiccation-tolerant Norway maple seeds. Post-translational modifications of PRXIIF in seeds at a 50% WC were detected via 2D electrophoresis and subsequent western blot analysis. The detected shift in the pI values (± 0.3) in A. pseudoplatanus was possibly caused by phosphorylation because several potential phosphorylation sites were predicted in silico for that protein. The gene and amino acid sequences were obtained and aligned with known sequences of other plant PRXIIF genes and proteins. High values of sequence identity were noted between the PRXIIF protein sequences of Acer species, Populus trichocarpa Torr. & A. Gray and Arabidopsis thaliana (L.) Heynh. The involvement of PRXIIF in defining the physiological differences between desiccation-tolerant and desiccation-sensitive Acer seeds is discussed in the context of its role in mitochondrial redox homeostasis.
Additional keywords: desiccation, seed.
References
Aalen RB (1999) Peroxiredoxin antioxidants in seed physiology. Seed Science Research 9, 285–295.| Peroxiredoxin antioxidants in seed physiology.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3cXpvF2kuw%3D%3D&md5=ed8d451fb9c6c6af8caec6e273d68155CAS |
Arc E, Galland M, Cueff G, Godin B, Lounifi I, Job D, Rajjou L (2011) Reboot the system thanks to protein post-translational modifications and proteome diversity: how quiescent seeds restart their metabolism to prepare seedling establishment. Proteomics 11, 1606–1618.
| Reboot the system thanks to protein post-translational modifications and proteome diversity: how quiescent seeds restart their metabolism to prepare seedling establishment.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3MXmslOhtr4%3D&md5=a094cf0cde35e916003da2136ce71e31CAS | 21433284PubMed |
Amme S, Matros A, Schlesier B, Mock HP (2006) Proteome analysis of cold stress response in Arabidopsis thaliana using DIGE-technology. Journal of Experimental Botany 57, 1537–1546.
| Proteome analysis of cold stress response in Arabidopsis thaliana using DIGE-technology.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD28XjslKkurc%3D&md5=4a57016fc7a85705e8c9b91250605dc6CAS | 16574749PubMed |
Altschul SF, Madden TL, Schäffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Research 25, 3382–3402.
Baier M, Dietz KJ (1997) The plant 2-Cys peroxiredoxin BAS1 is a nuclear-encoded chloroplast protein: its expressional regulation, phylogenetic origin, and implications for its specific physiological function in plants. The Plant Journal 12, 179–190.
| The plant 2-Cys peroxiredoxin BAS1 is a nuclear-encoded chloroplast protein: its expressional regulation, phylogenetic origin, and implications for its specific physiological function in plants.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK2sXlsFCrtLs%3D&md5=14fb8d805653e3cba544edde9378631cCAS | 9263459PubMed |
Baier M, Dietz KJ (2005) Chloroplasts as source and target of cellular redox regulation: a discussion on chloroplast redox signals in the context of plant physiology. Journal of Experimental Botany 56, 1449–1462.
| Chloroplasts as source and target of cellular redox regulation: a discussion on chloroplast redox signals in the context of plant physiology.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2MXktl2quro%3D&md5=8da5916b29f7ebd8f6b2353a6f223338CAS | 15863449PubMed |
Baier M, Noctor G, Foyer CH, Dietz KJ (2000) Antisense suppression of 2-Cysteine peroxiredoxin in Arabidopsis specifically enhances the activities and expression of enzymes associated with ascorbate metabolism but not glutathione metabolism. Plant Physiology 124, 823–832.
| Antisense suppression of 2-Cysteine peroxiredoxin in Arabidopsis specifically enhances the activities and expression of enzymes associated with ascorbate metabolism but not glutathione metabolism.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3cXnsF2rsbc%3D&md5=0a83df8dcd89ed1179a4a6f9caf12323CAS | 11027730PubMed |
Bailly CH (2004) Active oxygen species and antioxidants in seed biology. Seed Science Research 14, 93–107.
| Active oxygen species and antioxidants in seed biology.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2cXlvFSgt7o%3D&md5=21f3edbd39f38048179c81c59c180bdaCAS |
Bailly C, El-Maarouf-Bouteau H, Corbineau F (2008) From intracellular signaling networks to cell death: the dual role of reactive oxygen species in seed physiology. Comptes Rendus Biologies 331, 806–814.
| From intracellular signaling networks to cell death: the dual role of reactive oxygen species in seed physiology.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD1cXht1Shtr7J&md5=400d9c1bfe6b3325ac57af58a1a0ac3cCAS | 18926495PubMed |
Barranco-Medina S, Krell T, Finkemeier I, Sevilla F, Lazaro JJ, Dietz KJ (2007) Biochemical and molecular characterization of the mitochondrial peroxiredoxin Ps Prx IIF from Pisum sativum. Plant Physiology and Biochemistry 45, 729–739.
| Biochemical and molecular characterization of the mitochondrial peroxiredoxin Ps Prx IIF from Pisum sativum.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2sXhtFGrs7fL&md5=9313e67fc9a2c8a9dd5bb24679451980CAS | 17881238PubMed |
Berjak P, Pammenter NW (1997) Progress in the understanding and manipulation of desiccation-sensitive (recalcitrant) seeds. In ‘Basic and applied aspects of seed biology’. (Eds RH Ellis, M Black, AJ Murdoch, TD Hong) pp. 689–703. (Kluwer Academic Publishers: Dordrecht, The Netherlands)
Bernier-Villamor RL, Navarro E, Sevilla F, Lazaro JJ (2004) Cloning and characterization of a 2-Cys peroxiredoxin from Pisum sativum. Journal of Experimental Botany 55, 2191–2199.
| Cloning and characterization of a 2-Cys peroxiredoxin from Pisum sativum.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2cXnvVOksLk%3D&md5=780d0fe75888948724ac4427c4f913dcCAS |
Blom N, Sicheritz-Ponten T, Gupta R, Gammeltoft S, Brunak S (2004) Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence. Proteomics 4, 1633–1649.
| Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2cXkvFGitLg%3D&md5=be8d69c3b0af468560d20b1c448f7d6bCAS | 15174133PubMed |
Blum H, Beier H, Gross JH (1987) Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8, 93–99.
| Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaL2sXhsFagtLc%3D&md5=dec6fd261c8bff76706a26abc1759007CAS |
Brehelin C, Meyer EH, de Souris JP, Bonnard G, Meyer Y (2003) Resemblance and dissemblance of Arabidopsis type II peroxiredoxins: similar sequences for divergent gene expression, protein localization, and activity. Plant Physiology 132, 2045–2057.
| Resemblance and dissemblance of Arabidopsis type II peroxiredoxins: similar sequences for divergent gene expression, protein localization, and activity.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3sXmsVantLY%3D&md5=62de7874a7f5ee54d46079452897efabCAS | 12913160PubMed |
Buchanan BB, Balmer Y (2005) Redox regulation: a broadening horizon. Annual Review of Plant Biology 56, 187–220.
| Redox regulation: a broadening horizon.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2MXmtVaru7s%3D&md5=ef4c45b65b6d48a3d74ad050882b1b9dCAS | 15862094PubMed |
Chan HL, Gharbi S, Gaffney PR, Cramer R, Waterfield MD, Timms JF (2005) Proteomic analysis of redox- and ErbB2-dependent changes in mammary luminal epithelial cells using cysteine- and lysine-labelling two-dimensional difference gel electrophoresis. Proteomics 5, 2908–2926.
| Proteomic analysis of redox- and ErbB2-dependent changes in mammary luminal epithelial cells using cysteine- and lysine-labelling two-dimensional difference gel electrophoresis.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2MXnvVWhtbs%3D&md5=60169e75870b09b377f2524ac68ac350CAS | 15954156PubMed |
Chang TS, Jeong W, Choi SY, Yu S, Kang SW, Rhee SG (2002) Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation. Journal of Biological Chemistry 277, 25370–25376.
| Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD38XlsVWhsrY%3D&md5=46aa4487ddf9ee63739f4e1b8dd8ccbbCAS | 11986303PubMed |
Cheong NE, Choi YO, Lee KO, Kim WY, Jung BG, Chi YH, Jeong JS, Kim K, Cho MJ, Lee SY (1999) Molecular cloning, expression, and functional characterization of a 2Cys-peroxiredoxin in Chinese cabbage. Plant Molecular Biology 40, 825–834.
| Molecular cloning, expression, and functional characterization of a 2Cys-peroxiredoxin in Chinese cabbage.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK1MXmtFektbY%3D&md5=e72ea339d4096076b7ee1565f706e923CAS | 10487217PubMed |
Chevallet M, Wagner E, Luche S, van Dorsselaer A, Leize-Wagner E, Rabilloud T (2003) Regeneration of peroxiredoxins during recovery after oxidative stress: only some overoxidized peroxiredoxins can be reduced during recovery after oxidative stress. Journal of Biological Chemistry 278, 37146–37153.
| Regeneration of peroxiredoxins during recovery after oxidative stress: only some overoxidized peroxiredoxins can be reduced during recovery after oxidative stress.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3sXnsV2mtbc%3D&md5=85eaa87de0fb75e31fbace4af2062b2cCAS | 12853451PubMed |
De Gara L, Locato V, Dipierro S, De Pinto M (2010) Redox homeostasis in plants. The challenge of living with endogenous oxygen production. Respiratory Physiology & Neurobiology 173, S13–S19.
| Redox homeostasis in plants. The challenge of living with endogenous oxygen production.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3cXpvVOis70%3D&md5=de63cc2b22ad785bb119b08cba6b1c69CAS |
Declercq JP, Evrard C, Clippe A, Vander Stricht D, Bernard A, Knoops B (2001) Crystal structure of human peroxiredoxin5, a novel type of mammalian peroxiredoxin at 1.5 Å resolution. Journal of Molecular Biology 311, 751–759.
| Crystal structure of human peroxiredoxin5, a novel type of mammalian peroxiredoxin at 1.5 Å resolution.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3MXmtFGgtrY%3D&md5=3b038e3c761355d311f6b27c1998c83bCAS | 11518528PubMed |
Desican R, Hancock JT, Neill SJ (2005) Reactive oxygen species as signaling molecules. In ‘Antioxidants and reactive oxygen species in plants’. (Ed. N Smirnoff) pp. 166–97. (Blackwell Publishing: New York)
Dickie JB, May K, Morris SVA, Titley SE (1991) The effect of desiccation on seed survival in Acer platanoides L. and Acer pseudoplatanus L. Seed Science Research 1, 149–162.
| The effect of desiccation on seed survival in Acer platanoides L. and Acer pseudoplatanus L.Crossref | GoogleScholarGoogle Scholar |
Dietz KJ (2003) Redox regulation, redox signalling and redox homeostasis in plant cells. International Review of Cytology 228, 141–193.
| Redox regulation, redox signalling and redox homeostasis in plant cells.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2cXktlejtw%3D%3D&md5=f002a7145c529afc5f2a7f4e3895c0adCAS | 14667044PubMed |
Dietz KJ (2011) Peroxiredoxins in plants and cyanobacteria. Antioxidants & Redox Signalling 15, 1129–1159.
| Peroxiredoxins in plants and cyanobacteria.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3MXovFKlsbw%3D&md5=fb1e5edd4a22b9bb2049953e25a29c62CAS |
Dietz KJ, Horling J, Köning J, Baier M (2002) The function of the chloroplast 2-cysteine peroxiredoxin in peroxide detoxification and its regulation. Journal of Experimental Botany 53, 1321–1329.
| The function of the chloroplast 2-cysteine peroxiredoxin in peroxide detoxification and its regulation.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD38XktFSls7c%3D&md5=f6e13b6f9b908d9f9acfae2452b4a875CAS | 11997378PubMed |
Dietz KJ, Jacob S, Oelze ML, Laxa M, Tognetti V, Nunes De Miranda SM, Baier M, Finkemeier I (2006) The function of peroxiredoxins in plant organelle redox metabolism. Journal of Experimental Botany 57, 1697–1709.
| The function of peroxiredoxins in plant organelle redox metabolism.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD28XmsVaqsr4%3D&md5=661ed9e61987a126d15ea7853d8678edCAS | 16606633PubMed |
Finkemeier I, Goodman M, Lamkemeyer P, Kandlbinder A, Sweetlove LJ, Dietz KJ (2005) The mitochondrial type II peroxiredoxin F is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress. Journal of Biological Chemistry 280, 12168–12180.
| The mitochondrial type II peroxiredoxin F is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2MXislyhtr4%3D&md5=8bbd0ad9d93d6932b442dda790773bb1CAS | 15632145PubMed |
Foyer Ch, Noctor G (2005) Oxidant and antioxidant signaling in plants: a re-evaluation of the concept of oxidative stress in a physiological context. Plant, Cell & Environment 28, 1056–1071.
| Oxidant and antioxidant signaling in plants: a re-evaluation of the concept of oxidative stress in a physiological context.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2MXpslSgs70%3D&md5=081c2cef1cc8ab1223183f3a534fe008CAS |
Gama F, Keech O, Eymery F, Finkemeier I, Gelhaye E, Gardeström P, Dietz KJ, Rey P, Jacquot JP, Rouhier N (2007) The mitochondrial type II peroxiredoxin from poplar. Physiologia Plantarum 129, 196–206.
| The mitochondrial type II peroxiredoxin from poplar.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2sXhslKgt7o%3D&md5=e71e4df80a173ffb95a5f7619fc121e5CAS |
Groten K, Dutilleul C, van Heerden PD, Vanacker H, Bernard S, Finkemeier I, Dietz KJ, Foyer CH (2006) Redox regulation of peroxiredoxin and proteinases by ascorbate and thiols during pea root nodule senescence. FEBS Letters 580, 1269–1276.
| Redox regulation of peroxiredoxin and proteinases by ascorbate and thiols during pea root nodule senescence.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD28Xhs1Snsbs%3D&md5=a7e803d86c49abca03e5a1aedb0b61e7CAS | 16455082PubMed |
Haslekås C, Viken MK, Grini PE, Nygaard V, Nordgard SH, Trine JM, Aalen RB (2003) Seed 1-cysteine peroxiredoxin antioxidants are not involved in dormancy, but contribute to inhibition of germination during stress. Plant Physiology 133, 1148–1157.
| Seed 1-cysteine peroxiredoxin antioxidants are not involved in dormancy, but contribute to inhibition of germination during stress.Crossref | GoogleScholarGoogle Scholar | 14526116PubMed |
Heiber I, Ströher E, Raatz B, Busse I, Kahmann U, Bevan MW, Dietz KJ, Baier M (2007) The redox imbalanced mutants of Arabidopsis differentiate signaling pathways for redox regulation of chloroplast antioxidant enzymes. Plant Physiology 143, 1774–1788.
| The redox imbalanced mutants of Arabidopsis differentiate signaling pathways for redox regulation of chloroplast antioxidant enzymes.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2sXksFWjtb0%3D&md5=252673f5168add1e69ae3d3e94f2e92aCAS | 17337533PubMed |
Hong TD, Ellis EH (1990) A comparison of maturation drying, germination and desiccation tolerance between developing seeds of Acer pseudoplatanus L. and Acer platanoides L. New Phytologist 116, 589–596.
| A comparison of maturation drying, germination and desiccation tolerance between developing seeds of Acer pseudoplatanus L. and Acer platanoides L.Crossref | GoogleScholarGoogle Scholar |
Horling F, König J, Dietz KJ (2002) Type II peroxiredoxin C, a member of the peroxiredoxin family of Arabidopsis thaliana: its expression and activity in comparison with other peroxiredoxins. Plant Physiology and Biochemistry 40, 491–499.
| Type II peroxiredoxin C, a member of the peroxiredoxin family of Arabidopsis thaliana: its expression and activity in comparison with other peroxiredoxins.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD38XntVajtb8%3D&md5=b3ef9d972d7c08018db0347733d39215CAS |
Horling F, Lamkemeyer P, König J, Finkemeier I, Baier M, Kandlbinder A, Baier M, Dietz KJ (2003) Divergent light-, ascorbate- and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis thaliana. Plant Physiology 131, 317–325.
| Divergent light-, ascorbate- and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis thaliana.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3sXnvVGntA%3D%3D&md5=3a48aaf1dfb5ef14609d122a7c82fa8eCAS | 12529539PubMed |
Huang HD, Lee TY, Tseng SW, Horng JT (2005) KinasePhos: a web tool for identifying protein kinase-specific phosphorylation sites. Nucleic Acids Research 33, W226–W229.
| KinasePhos: a web tool for identifying protein kinase-specific phosphorylation sites.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2MXlslyqtLo%3D&md5=e07b710329a3b37f8a9f08a3a9409bb9CAS | 15980458PubMed |
Ingram J, Bartels D (1996) The molecular basis of dehydration tolerance in plants. Annual Review of Plant Physiology and Plant Molecular Biology 47, 377–403.
| The molecular basis of dehydration tolerance in plants.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK28XjtlWgtr0%3D&md5=fb5eb32eb84894ab5e9e4ec3bd6114a0CAS | 15012294PubMed |
ISTA (1999) International rules for seed testing. Rules. Seed Science Research 27, 155–199.
Jahnel H (1955) The stratification of forest seed. Angewandte Botanik 29, 139–141.
Kalemba EM, Pukacka S (2012) Association of protective proteins with dehydration and desiccation of orthodox and recalcitrant category seeds of three Acer genus species. Journal of Plant Growth Regulation 31, 351–362.
| Association of protective proteins with dehydration and desiccation of orthodox and recalcitrant category seeds of three Acer genus species.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC38XhtFWnsLjN&md5=89f9ed0cc2ea196afd0c4d2de699ca4cCAS |
Katsube T, Kurisaka N, Ogawa M, Maruyama N, Ohtsuka R, Utsumi S, Takaiwa F (1999) Accumulation of soybean glycinin and its assembly with the glutelins in rice. Plant Physiology 120, 1063–1074.
| Accumulation of soybean glycinin and its assembly with the glutelins in rice.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK1MXls12rsLY%3D&md5=fb5629c7218dd0917963c72c488a1e2bCAS | 10444090PubMed |
Kranner I, Minibayeva FV, Beckett RB, Seal ChE (2010) What is stress? Concepts, definitions and applications in seed science. New Phytologist 188, 655–673.
| What is stress? Concepts, definitions and applications in seed science.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3cXhsFKnur%2FK&md5=f6772287018a8410e34e31afe93e1fffCAS | 20854396PubMed |
Lopato S, Langridge P (2011) Engineering stress tolerance in cereals using DREB/CBF genes: outcomes, problems and perspectives. ISB News Report.
Marchler-Bauer A, Lu S, Anderson JB, Chitsaz F, Derbyshire MK, DeWeese-Scott C, Fong JH, Geer LY, Geer RC, Gonzales NR, Gwadz M, Hurwitz DI, Jackson JD, Ke Z, Lanczycki CJ, Lu F, Marchler GH, Mullokandov M, Omelchenko MV, Robertson CL, Song JS, Thanki N, Yamashita RA, Zhang D, Zhang N, Zheng C, Bryant SH (2011) CDD: a Conserved Domain Database for the functional annotation of proteins. Nucleic Acids Research 39, D225–D229.
| CDD: a Conserved Domain Database for the functional annotation of proteins.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3sXivF2ltb8%3D&md5=c9dd751068a10e43f183fe5f26ed319dCAS | 21109532PubMed |
Mittler R, Poulos TL (2005) Ascorbate peroxidase. In ‘Antioxidants and reactive oxygen species in plants’. (Ed. N Smirnoff) pp. 87–100. (Blackwell Publishing: Oxford)
Muthuramalingam M, Seidel T, Laxa M, de Miranda SMN, Gärtner F, Ströher E, Kandlbinder A, Dietz KJ (2009) Multiple redox and non-redox interactions define 2-Cys peroxiredoxin as a regulatory hub in the chloroplast. Molecular Plant 2, 1273–1288.
| Multiple redox and non-redox interactions define 2-Cys peroxiredoxin as a regulatory hub in the chloroplast.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD1MXhsV2itL%2FL&md5=35e0b7255a2a7997e7e8a23b64836c27CAS | 19995730PubMed |
Nedeva D, Nikolova A (1997) Desiccation tolerance in developing seeds. Bulgarian Journal of Plant Physiology 2, 100–113.
Obenauer JC, Cantley LC, Yaffe MB (2003) Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs. Nucleic Acids Research 31, 3635–3641.
| Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3sXltVWju74%3D&md5=4ad20ba0ef32aa9df07550817465f238CAS | 12824383PubMed |
Oelze ML, Kandlbinder A, Dietz KJ (2008) Redox regulation and over reduction control in the photosynthesizing cell: complexity in redox regulatory networks. Biochimica et Biophysica Acta 1780, 1261–1272.
| Redox regulation and over reduction control in the photosynthesizing cell: complexity in redox regulatory networks.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD1cXhtVarsbfI&md5=a32c6744ae4938196c88da49848e838dCAS | 18439433PubMed |
Pawłowski TA (2009) Proteome analysis of Norway maple (Acer platanoides L.) seeds dormancy breaking and germination: influence of abscisic and gibberellic acid. BMC Plant Biology 9, 48
| Proteome analysis of Norway maple (Acer platanoides L.) seeds dormancy breaking and germination: influence of abscisic and gibberellic acid.Crossref | GoogleScholarGoogle Scholar | 19413897PubMed |
Pena-Ahumada A, Kahmann U, Dietz KJ, Baier M (2006) Regulation of peroxiredoxin expression versus expression of Halliwell-Asada-cycle enzymes during early seedling development of Arabidopsis thaliana. Photosynthesis Research 89, 99–112.
| Regulation of peroxiredoxin expression versus expression of Halliwell-Asada-cycle enzymes during early seedling development of Arabidopsis thaliana.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD28XpvVarsrw%3D&md5=b36518c133dfd9da5832e558cde01828CAS | 16915352PubMed |
Pukacka S (1998) Changes in membrane fatty acid composition during desiccation of seeds of silver maple. Seed Science and Technology 26, 535–540.
Pukacka S, Czubak A (1998) The effect of desiccation on viability and membrane lipid composition of Acer pseudoplatanus seeds. Acta Societatis Botanicorum Poloniae 67, 249–252.
Pukacka S, Ratajczak E (2007) Ascorbate and glutathione metabolism during development and desiccation of orthodox and recalcitrant seeds of the genus Acer. Functional Plant Biology 34, 601–613.
| Ascorbate and glutathione metabolism during development and desiccation of orthodox and recalcitrant seeds of the genus Acer.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2sXos1Kgurc%3D&md5=7e1a0399badc2192b657d2b815cf27a0CAS |
Pukacka S, Wójkiewicz E (2002) Carbohydrate metabolism in Norway maple and sycamore seeds in relation to desiccation tolerance. Journal of Plant Physiology 159, 273–279.
| Carbohydrate metabolism in Norway maple and sycamore seeds in relation to desiccation tolerance.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD38XivFygu78%3D&md5=ddd3fc8d62887e4f37a1038496bb8edeCAS |
Pukacka S, Ratajczak E, Kalemba E (2011) The protective role of selenium in recalcitrant Acer saccharinum L. seeds subjected to desiccation. Journal of Plant Physiology 168, 220–225.
| The protective role of selenium in recalcitrant Acer saccharinum L. seeds subjected to desiccation.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3cXhs1ajtbnM&md5=46f89f56d5911056d45c6b9c4ae96cc7CAS | 20933296PubMed |
Rabilloud T, Heller M, Gasnier F, Luche S, Rey C, Aebersold R, Benahmed M, Louisot P, Lunardi J (2002) Proteomics analysis of cellular response to oxidative stress. Journal of Biological Chemistry 277, 19396–19401.
| Proteomics analysis of cellular response to oxidative stress.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD38XksVWltbo%3D&md5=187d60b95c7d49fd186116515a8a2f4eCAS | 11904290PubMed |
Roberts EH (1973) Predicting the storage life of seeds. Seed Science and Technology 1, 499–514.
Rouhier N, Jacquot JP (2005) The plant multigenic family of thiol peroxidases. Free Radical Biology & Medicine 38, 1413–1421.
| The plant multigenic family of thiol peroxidases.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2MXktFGitLc%3D&md5=90e9e50bf82b1e1dc2cf195f8197efe0CAS |
Sakamoto A, Tsukamoto S, Yamamoto H, Ueda-Hashimoto M, Takahashi M, Suzuki H, Morikawa H (2003) Functional complementation in yeast reveals a protective role of chloroplast 2-Cys peroxiredoxin against reactive nitrogen species. The Plant Journal 33, 841–851.
| Functional complementation in yeast reveals a protective role of chloroplast 2-Cys peroxiredoxin against reactive nitrogen species.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3sXis1Gls7g%3D&md5=a859c51c8afa203bf1780e6843e4defeCAS | 12609026PubMed |
Schafer FQ, Buettner GR (2001) Redox environment of cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radical Biology & Medicine 30, 1191–1212.
| Redox environment of cell as viewed through the redox state of the glutathione disulfide/glutathione couple.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3MXjsFegt78%3D&md5=0c800ea16e9fe1d0b0bea60cbb630f44CAS |
Smirnoff N, Bryant JA (1999) DREB takes the stress out of growing up. Nature Biotechnology 17, 229–230.
| DREB takes the stress out of growing up.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK1MXhs1Chsrc%3D&md5=31e92682e38b4c347bbd0c58164f8d75CAS | 10096286PubMed |
Ströher E, Dietz KJ (2006) Concepts and approaches towards understanding the cellular redox proteome. Plant Biology 8, 407–418.
| Concepts and approaches towards understanding the cellular redox proteome.Crossref | GoogleScholarGoogle Scholar | 16906481PubMed |
Ströher E, Dietz KJ (2008) The dynamic thiol-disulfide redox proteome of the Arabidopsis thaliana chloroplast as revealed by differential electrophoretic mobility. Physiologia Plantarum 133, 566–583.
| The dynamic thiol-disulfide redox proteome of the Arabidopsis thaliana chloroplast as revealed by differential electrophoretic mobility.Crossref | GoogleScholarGoogle Scholar | 18433418PubMed |
van der Linde K, Gutsche N, Leffers HM, Lindermayr Ch, Müller B, Holtgrefe S, Scheibe R (2011) Regulation of plant cytosolic aldolase functions by redox-modifications. Plant Physiology and Biochemistry 49, 946–957.
| Regulation of plant cytosolic aldolase functions by redox-modifications.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3MXhtV2qu7zL&md5=d69c7f8accb8840d95a42a4d9e638537CAS | 21782461PubMed |
Wan J, Kang S, Tang C, Yan J, Ren Y, Liu J, Gao X, Banerjee A, Ellis LBM, Li T (2008) Meta-prediction of phosphorylation sites with weighted voting and restricted grid search parameter selection. Nucleic Acids Research 36, 1–11.
Wang Z, Martin J, Abubucker S, Yin Y, Gasser RB, Mitreva M (2009) Systematic analysis of insertions and deletions specific to nematode proteins and their proposed functional and evolutionary relevance. BMC Evolutionary Biology 9, 1–14.
Watt SA, Wilke A, Patschkowski T, Niehaus K (2005) Comprehensive analysis of the extracellular proteins from Xanthomonas campestris pv. campestris B100. Proteomics 5, 153–167.
| Comprehensive analysis of the extracellular proteins from Xanthomonas campestris pv. campestris B100.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2MXhtleis7s%3D&md5=ba0dc99180cceb6ad2ff4cc0e0517513CAS | 15619296PubMed |
Woo HA, Yim SH, Shin DH, Kang D, Yu DY, Rhee SG (2010) Inactivation of peroxiredoxin I by phosphorylation allows localized H2O2 accumulation for cell signaling. Cell 140, 517–528.
| Inactivation of peroxiredoxin I by phosphorylation allows localized H2O2 accumulation for cell signaling.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3cXlt1Klt7w%3D&md5=a55c0683b0bae4dc68ed0af0f7e199caCAS | 20178744PubMed |
Wood ZA, Poole LB, Hantgan RR, Karplus PA (2002) Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins. Biochemistry 41, 5493–5504.
| Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD38XisVOis7Y%3D&md5=c8a7928baf5126efc0bca259dca98e18CAS | 11969410PubMed |
Yano H, Wong JH, Lee YM, Cho MJ, Buchanan BB (2001) A strategy for the identification of proteins targeted by thioredoxin. Proceedings of the National Academy of Sciences of the United States of America 98, 4794–4799.
| A strategy for the identification of proteins targeted by thioredoxin.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3MXjtVantbg%3D&md5=26b5a6213a67f50b3715c43c4e802f77CAS | 11274350PubMed |
