scholarly journals Triazine Probes Target Ascorbate Peroxidases in Plants

2019 ◽  
Vol 180 (4) ◽  
pp. 1848-1859
Author(s):  
Kyoko Morimoto ◽  
Kyle S. Cole ◽  
Jiorgos Kourelis ◽  
Collin H. Witt ◽  
Daniel Brown ◽  
...  
Keyword(s):  
Ascorbate Peroxidases

Differential Expression of Two Cytosolic Ascorbate Peroxidases and Two Superoxide Dismutase Genes in Response to Abiotic Stress in Rice

Rice Science ◽  
2011 ◽  
Vol 18 (3) ◽  
pp. 157-166 ◽  
Author(s):  
Shigeto MORITA ◽  
Shinya NAKATANI ◽  
Tomokazu KOSHIBA ◽  
Takehiroy MASUMURA ◽  
Yasunari OGIHARA ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Abiotic Stress ◽  
Differential Expression ◽  
Ascorbate Peroxidases

scholarly journals Silenced rice in both cytosolic ascorbate peroxidases displays pre-acclimation to cope with oxidative stress induced by 3-aminotriazole-inhibited catalase

2016 ◽  
Vol 201 ◽  
pp. 17-27 ◽  
Author(s):  
Aurenivia Bonifacio ◽  
Fabrício E.L. Carvalho ◽  
Marcio O. Martins ◽  
Milton C. Lima Neto ◽  
Juliana R. Cunha ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Ascorbate Peroxidases

Stromal and thylakoid-bound ascorbate peroxidases in NaCl-treated wheat

1998 ◽  
Vol 104 (4) ◽  
pp. 735-740 ◽  
Author(s):  
Sandra Meneguzzo ◽  
Cristina L.M. Sgherri ◽  
Flavia Navari-Izzo ◽  
Riccardo Izzo
Keyword(s):  
Ascorbate Peroxidases

The knockdown of chloroplastic ascorbate peroxidases reveals its regulatory role in the photosynthesis and protection under photo-oxidative stress in rice

Plant Science ◽  
2014 ◽  
Vol 214 ◽  
pp. 74-87 ◽  
Author(s):  
Andréia Caverzan ◽  
Aurenivia Bonifacio ◽  
Fabricio E.L. Carvalho ◽  
Claudia M.B. Andrade ◽  
Gisele Passaia ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Regulatory Role ◽  
Ascorbate Peroxidases

Diverse roles for chloroplast stromal and thylakoid-bound ascorbate peroxidases in plant stress responses

2008 ◽  
Vol 412 (2) ◽  
pp. 275-285 ◽  
Author(s):  
Saijaliisa Kangasjärvi ◽  
Anna Lepistö ◽  
Kati Hännikäinen ◽  
Mirva Piippo ◽  
Eeva-Maria Luomala ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Stress Responses ◽  
Double Mutant ◽  
Light Stress ◽  
Plant Stress ◽  
Optimal Growth ◽  
Sudden Onset ◽  
High Light ◽  
Mature Leaves ◽  
Ascorbate Peroxidases

Photosynthetic light reactions comprise a significant source of hydrogen peroxide (H2O2) in illuminated leaves. APXs (ascorbate peroxidases) reduce H2O2 to water and play an important role in the antioxidant system of plants. In the present study we addressed the significance of chloroplast APXs in stress tolerance and signalling in Arabidopsis thaliana. To this end, T-DNA (transfer DNA) insertion mutants tapx, sapx and tapx sapx, lacking the tAPX (thylakoid-bound APX), sAPX (stromal APX) or both respectively, were characterized. Photo-oxidative stress during germination led to bleaching of chloroplasts in sapx single-mutant and particularly in the tapx sapx double-mutant plants, whereas the greening process of wild-type and tapx plants was only partially impaired. Mature leaves of tapx sapx double mutants were also susceptible to short-term photo-oxidative stress induced by high light or methyl viologen treatments. After a 2-week acclimation period under high light or under low temperature, none of the mutants exhibited enhanced stress symptoms. Immunoblot analysis revealed that high-light-stress-acclimated tapx sapx double mutants compensated for the absence of tAPX and sAPX by increasing the level of 2-cysteine peroxiredoxin. Furthermore, the absence of tAPX and sAPX induced alterations in the transcriptomic profile of tapx sapx double-mutant plants already under quite optimal growth conditions. We conclude that sAPX is particularly important for photoprotection during the early greening process. In mature leaves, tAPX and sAPX are functionally redundant, and crucial upon sudden onset of oxidative stress. Moreover, chloroplast APXs contribute to chloroplast retrograde signalling pathways upon slight fluctuations in the accumulation of H2O2 in chloroplasts.

Sequence Variability of Nine Cytosolic Ascorbate Peroxidases in Polyploid Strawberry

DNA Sequence ◽  
2001 ◽  
Vol 11 (6) ◽  
pp. 475-484 ◽  
Author(s):  
Byung-Hyun Lee ◽  
Jinki Jo ◽  
Won-Il Chung
Keyword(s):  
Sequence Variability ◽  
Ascorbate Peroxidases

scholarly journals From sequence analysis of three novel ascorbate peroxidases from Arabidopsis thaliana to structure, function and evolution of seven types of ascorbate peroxidase

1997 ◽  
Vol 326 (2) ◽  
pp. 305-310 ◽  
Author(s):  
Hans M. JESPERSEN ◽  
Inger V. H. KJÆRSGÅRD ◽  
Lars ØSTERGAARD ◽  
Karen G. WELINDER
Keyword(s):  
Ascorbate Peroxidase ◽  
Sequence Data ◽  
Duplication Event ◽  
Monovalent Cation ◽  
Early Gene ◽  
Active Site Residues ◽  
Cation Site ◽  
Ascorbate Peroxidases ◽  
Complete Sequencing ◽  
Membrane Spanning

Ascorbate peroxidases are haem proteins that efficiently scavenge H2O2 in the cytosol and chloroplasts of plants. Database analyses retrieved 52 expressed sequence tags coding for Arabidopsis thalianaascorbate peroxidases. Complete sequencing of non-redundant clones revealed three novel types in addition to the two cytosol types described previously in Arabidopsis. Analysis of sequence data available for all plant ascorbate peroxidases resulted in the following classification: two types of cytosol soluble ascorbate peroxidase designated cs1 and cs2; three types of cytosol membrane-bound ascorbate peroxidase, namely cm1, bound to microbodies via a C-terminal membrane-spanning segment, and cm2 and cm3, both of unknown location; two types of chloroplast ascorbate peroxidase with N-terminal transit sequences, the stromal ascorbate peroxidase (chs), and the thylakoid-bound ascorbate peroxidase showing a C-terminal transmembrane segment and designated cht. Further comparison of the patterns of conserved residues and the crystal structure of pea ascorbate peroxidase showed that active site residues are conserved, and three peptide segments implicated in interaction with reducing substrate are similar, excepting cm2 and cm3 types. A change of Phe-175 in cytosol types to Trp-175 in chloroplast types might explain the greater ascorbate specificity of chloroplast compared with cytosol ascorbate peroxidases. Residues involved in homodimeric subunit interaction are conserved only in cs1, cs2 and cm1 types. The proximal cation (K+)-binding site observed in pea ascorbate peroxidase seems to be conserved. In addition, cm1, cm2, cm3, chs and cht ascorbate peroxidases contain Asp-43, Asn-57 and Ser-59, indicative of a distal monovalent cation site. The data support the hypothesis that present-day peroxidases evolved by an early gene duplication event.

Ascorbate Peroxidases: Scavengers or Sensors of Hydrogen Peroxide Signaling?

2019 ◽  
pp. 85-115 ◽  
Author(s):  
Andréia Caverzan ◽  
Douglas Jardim-Messeder ◽  
Ana Luiza Paiva ◽  
Marcia Margis-Pinheiro
Keyword(s):  
Hydrogen Peroxide ◽  
Ascorbate Peroxidases
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