Os02g0553200

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Annotated Information

Function

Ascorbate peroxidase (APx; EC 1.11.1.11) plays an important role in scavenging the toxic effects of H2O2 in higher plants. Eight types of APx have been described for Oryza sativa: two cytosolic (OsAPx1 and OsAPx2), two putative peroxisomal (OsAPx3 and OsAPx4), and four chloroplastic isoforms (OsAPx5, OsAPx6, OsAPx7 and OsAPx8).[1]

The effect of Flu on the expression of OsAPx8 and increase in APx activity was reversed by the application of ABA. It appears that NaCl-enhanced expression of OsAPx8 in rice roots is mediated through an accumulation of ABA. Evidence is provided to show that Na+ but not Cl– is required for enhancing OsAPx8 expression, APx activity, and ABA accumulation in rice roots treated with NaCl. H2O2 treatment resulted in an enhancement of OsAPx8 induction but no accumulation of ABA. Diphenylene iodonium treatment, which is known to inhibit NaCl-induced accumulation of H2O2 in rice roots, did not suppress OsAPx8 induction and ABA accumulation by NaCl. It appears that H2O2 is not involved in the regulation of NaCl-induced OsAPx8 expression in rice roots.).[2].The results obtained so far seem to conclude that NaCl-inducing OsAPx8 expression in rice roots is associated with ionic but not osmotic component.[1]

Expression

In stress-induced gene expression, ABA has been thought to be a candidate for a signal transducer. The present study indicated that ABA was involved in regulating the expression of OsAPx8 in rice roots by NaCl. This conclusion was based on the following observations:(i) NaCl treatment resulted in an increase in the endogenous level of ABA (Fig. 2B) and the induction of OsAPx8 expression in rice roots (Fig. 2A); (ii) the expression of OsAPx8 in rice roots was enhanced by exogenous ABA (Fig. 3A); (iii) the increase in ABA levels due to NaCl preceded the enhancement of OsAPx8 expression (Fig. 2); (iv) Flu treatment reduced the ABA level, as well as NaCl-induced OsAPx8 expression (Fig.4); and (v) the effect of Flu on the reduction of OsAPx8 expression caused by NaCl can be reversed by the application of ABA (Fig. 4A). The present results suggest that NaCl-enhanced OsAPx8 expression is mediated through ABA accumulation in rice roots..[2]


Figure 1. Expression(from reference) [2].. Figure 2. Expression(from reference) [2].. Figure 3. Expression(from reference) [2].. Figure 4. Expression(from reference) [2].. Figure 5. Expression(from reference) [2].. Figure 6. Expression(from reference) [2]..

Knowledge Extension

Figure 7. Expression(from reference) [2].

Soil salinity, particularly due to NaCl, can be considered as the single most widespread soil toxicity problem that global rice production faces at present. Salinity influences a number of physiological processes. These processes include photosynthesis, nutrient uptake, water absorption, root growth, and cellular metabolism.

Roots play a number of important roles during plant growth and development, and typically are the first and critical part of the plant to encounter soil salinity. When growing in saline soil, roots have to cope with two types of stress. The first of these is an osmotic stress resulting from salt concentration in the soil that results in lowered water potential and a consequent loss of cell turgor in roots. The second is ionic stress induced by changes in the concentrations of Na+, Cl-, or both in the root growing medium and within root tissues. In addition to its known components of osmotic stress and ion toxicity, salt stress is also manifested as an oxidative stress, all of which contribute to its deleterious effects.

The increase in reactive oxygen species (ROS) seems to occur as a response to most, if not all, abiotic stresses including drought and salinity. To minimize and/or to protect against the toxic effects of these damaging ROS, cells have evolved highly regulated enzymatic and non-enzymatic mechanisms to keep a balance between ROS production and destruction in order to maintain cellular redox homeostasis. ROS-scavenging enzymes include superoxide dismutase, ascorbate peroxidase (APx), glutathione reductase, and catalase.

APx (EC 1.11.1.11) belongs to the class I haemcontaining peroxidases found in higher plants and catalyses the conversion of H2O2 to H2O and O2 using ascorbate as the specific electron donor. It plays an important role in scavenging and in protecting cells against the toxic effects of H2O2 in higher plants. The fact that APx has a high affinity for H2O2 and is able to detoxify low concentrations of H2O2, whereas catalase has a high reaction rate but a low affinity for H2O2, renders APx an ideal candidate for tight regulation of H2O2. APx is located in different cellular compartments. Eight types of APx have been described for Oryza sativa: two cytosolic (OsAPx1 and OsAPx2), two putative peroxisomal (OsAPx3 and OsAPx4), and four chloroplastic isoforms (OsAPx5, OsAPx6, OsAPx7, and OsAPx8).[2]

Labs working on this gene

1 Department of Agricultural Chemistry and Institute of Biotechnology, National Taiwan University, Taipei, Taiwan, China.[1] [2] [3]

2 Department of Agronomy, National Taiwan University, Taipei, Taiwan, China.[1] [2] [3] [4]

3 Institute of Biotechnology, National Taiwan University, Taipei, Taiwan, China.[3]

4 Department of Genetics, Federal University of Rio Grande do Sul, Brazil.[5]

5 Biotechnology Center, Federal University of Rio Grande do Sul, Brazil.[5]

6 Department of Botany, Federal University of Rio Grande do Sul, Brazil.[5]

7 Department of Biochemistry and Molecular Biology, Federal University of Ceará, Brazil.[5]

8 Department of Biophysics, Federal University of Rio Grande do Sul, Brazil.[5]

9 Laborato´ rio de Gene´ tica Molecular Vegetal, Departamento de Gene´ tica, UFRJ, 21944-970 Rio de Janeiro, Brasil.[6]

10 Departamento de Bioquı´mica, Instituto de Quı´mica, UFRJ, 21944-970, Rio de Janeiro, Brasil.[6]

References

<references>

Felipe Karam Teixeira, Larissa Menezes-Benavente, Roge´ rio Margis, et al. Analysis of the Molecular Evolutionary History of the Ascorbate Peroxidase Gene Family: Inferences from the Rice Genome. Journal of Molecular Evolution, 2004, 59: 761-770.

Structured Information

Gene Name

Os02g0553200

Description

Similar to Thylakoid-bound ascorbate peroxidase (EC 1.11.1.11) (Fragment)

Version

NM_001053646.1 GI:115446662 GeneID:4329643

Length

3693 bp

Definition

Oryza sativa Japonica Group Os02g0553200, complete gene.

Source

Oryza sativa Japonica Group

 ORGANISM  Oryza sativa Japonica Group
           Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
           Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
           clade; Ehrhartoideae; Oryzeae; Oryza.
Chromosome

Chromosome 2

Location

Chromosome 2:21726247..21729939

Sequence Coding Region

21726478..21726630,21726710..21726937,21727437..21727541,21727616..21727693,21727776..21727850
,21728505..21728591,21728684..21728751,21728864..21728951,21729051..21729151
,21729261..21729381,21729476..21729637,21729739..21729909

Expression

GEO Profiles:Os02g0553200

Genome Context

<gbrowseImage1> name=NC_008395:21726247..21729939 source=RiceChromosome02 preset=GeneLocation </gbrowseImage1>

Gene Structure

<gbrowseImage2> name=NC_008395:21726247..21729939 source=RiceChromosome02 preset=GeneLocation </gbrowseImage2>

Coding Sequence

<cdnaseq>atggcggagcgcatcgccgcctccctcctcccggctgcctcgccctcgcctgctccgtcccctccccccccgcgcccccgcgtctccgccgcggccgccgcctccttcccatgctgctccaccagcgccggcggcctccgcctccgctcccgcccgtctcgcttcccgcagaaggctgcgacgacgaggagcgggcgcgccggcgcgggggcgcgggcggtggtccggtgcatggcggcggcggcggtggcggcgtccgacgcggcgcagctcaagagcgcccgggaggacatcagggagatcctcaagaccacctactgccaccccatcatggtccgtcttgggtggcacgattctggcacgtacgacaagaacatcgaggagtggccgcagaggggcggagccgacgggagcttgagatttgacgccgaattgagccacggagccaatgctggtctgattaatgctttgaagcttatccaaccaatcaaggacaaatacccgggtataacttatgctgatttgttccagttggcaagtgctacagcaattgaggaagctggtgggccgaaaattccaatgaaatatggacgagttgatgtcacagcagctgagcagtgcccaccagaggggaggcttcctgatgccggtccacgtgtgcccgctgatcatcttagggaggtattctacaggatgggccttgatgacaaggaaattgttgcattatctggagcacacacacttggaagatcaagacctgacaggagtggctggggaaagccagaaacaaaatatactaaggatgggcctggtgaacctggagggcaatcatggacagttgaatggttgaagtttgataacagttacttcaaggacataaaagagcaaagggaccaggatcttctagtgctacccacagatgctgcattatttgaggatccgtccttcaaggtatatgccgaaaaatatgcagaggatcaggaggcattctttaaagactacgctgaagctcatgctaaactgagcgaccttggtgcaaagttcgatccacctgagggattttcactggacgatgaaccagccgtcgaagagaaggatcctgaaccagcaccagcgccagcagcagcaccaccacctccaccagtcgaggagaagaaggaagctgaaccaactccagtaccagtaacggtaggagcagcagtggcatcatcgccagcggatgacaacaacggtgcagcaccgcaaccagagcccttcgtcgctgcgaaatactcctacggaaagaaggagctgtcggactcgatgaagcagaagatcagggcggagtacgagggattcggaggcagcccggacaagcctctgcagtccaactacttcctcaacatcatgctcttgatcggagggctggccttcttgacgtctctgctcgggagctga</cdnaseq>

Protein Sequence

<aaseq>MAERIAASLLPAASPSPAPSPPPPRPRVSAAAAASFPCCSTSAG GLRLRSRPSRFPQKAATTRSGRAGAGARAVVRCMAAAAVAASDAAQLKSAREDIREIL KTTYCHPIMVRLGWHDSGTYDKNIEEWPQRGGADGSLRFDAELSHGANAGLINALKLI QPIKDKYPGITYADLFQLASATAIEEAGGPKIPMKYGRVDVTAAEQCPPEGRLPDAGP RVPADHLREVFYRMGLDDKEIVALSGAHTLGRSRPDRSGWGKPETKYTKDGPGEPGGQ SWTVEWLKFDNSYFKDIKEQRDQDLLVLPTDAALFEDPSFKVYAEKYAEDQEAFFKDY AEAHAKLSDLGAKFDPPEGFSLDDEPAVEEKDPEPAPAPAAAPPPPPVEEKKEAEPTP VPVTVGAAVASSPADDNNGAAPQPEPFVAAKYSYGKKELSDSMKQKIRAEYEGFGGSP DKPLQSNYFLNIMLLIGGLAFLTSLLGS</aaseq>

Gene Sequence

<dnaseqindica>3310..3462#3003..3230#2399..2503#2247..2324#2090..2164#1349..1435#1189..1256#989..1076#789..889#559..679#303..464#31..201#aaaaactcactcgactcgagcgcgcgcgccatggcggagcgcatcgccgcctccctcctcccggctgcctcgccctcgcctgctccgtcccctccccccccgcgcccccgcgtctccgccgcggccgccgcctccttcccatgctgctccaccagcgccggcggcctccgcctccgctcccgcccgtctcgcttcccgcaggttcgcaatagttttagctcggctcgtgtttttttttttttgggggtggggggggggttgaatcgaggtgttctgagttgactgatgcgtggcacctgcagaaggctgcgacgacgaggagcgggcgcgccggcgcgggggcgcgggcggtggtccggtgcatggcggcggcggcggtggcggcgtccgacgcggcgcagctcaagagcgcccgggaggacatcagggagatcctcaagaccacctactgccaccccatcatggtacggaacgcccgcgccatctcagctctcgcatccatatgaacagagaagagtcagagatgatgaaatcctgcgatcctgctaccatgtacaggtccgtcttgggtggcacgattctggcacgtacgacaagaacatcgaggagtggccgcagaggggcggagccgacgggagcttgagatttgacgccgaattgagccacggagccaatgctggtacttaatttctcgtgtctcggcagtgcaatttcgaattcaggaaattcgtggagtaatcgtgctgatttccttcataatcgtatggttttggttggaattttgataggtctgattaatgctttgaagcttatccaaccaatcaaggacaaatacccgggtataacttatgctgatttgttccagttggcaagtgctacagcaattgaggtctcagacttcttctctctgctctagtgactttgctagatattttttggatgatcggtagtctatgtgcttgaatcttttgagaaaaatttcttgcaggaagctggtgggccgaaaattccaatgaaatatggacgagttgatgtcacagcagctgagcagtgcccaccagaggggaggcttcctggtcagtgtttccattaagttcttcattctgtttctgatcaacgtttgcatttatgaattgtgagaggaacttatcaaagagtgaccttctggtgttgataaatgccccccagatgccggtccacgtgtgcccgctgatcatcttagggaggtattctacaggatgggccttgatgacaaggtgtggatgatgcaaaaaagaaattagttgcctatctgctatttgttcttcatgtatgttgtataaccatttcttttggactatttatgcaggaaattgttgcattatctggagcacacacacttggaagatcaagacctgacaggagtggctggggaaagccagaaacaaaatatactgtatgttttcttgtccactttggaaactcaacaggaaaaataagttattttcagcagtaggaagttctaggcatggccagaccttcaatgttctacactctgggtatagaatattacatttttggggcatttgcaaatttgccaccggttttttcaatattgcaaggatgctactcgaatgacagttctagtgatatttttgcaattttctagtggcagttttgcaataacgattcaaagtagtggtaaatttgcaattgcccctacattttttgagacattcaggcagaggtgaaaacaatgcatgtacttttttgtgttatcttgtaagtaagcaccatattatgcttttaaaatccgtgaatactttgtccttatgctgtaaataaataatgttttaattcaggattttacaaaatgggttatccttacgtttcttttgtatgcatataatggtaaaatagaattaggatgctaagaacttcatagctaacaactttgtcattctctaagccctgatacttctctgtggggaaatgaagattaacttttcgatgcaatcttaccttaatcacaccagcacaatagcaaatcagattagtttcagttttcagactgacatttaaaggtggcttctattattgtggtctacagaaggatgggcctggtgaacctggagggcaatcatggacagttgaatggttgaagtttgataacagttacttcaaggtgtgttagcattttgtcatggtttacaaaattatttttttcatttgaatatgtgatgattcagctgatgataatgtttcaggacataaaagagcaaagggaccaggatcttctagtgctacccacagatgctgcattatttgaggatccgtccttcaaggttatttggttgtgctcaatttgtggcttgaatagctcataggtcactgtctgaaatatctgcaacatatgcaggtatatgccgaaaaatatgcagaggatcaggaggcattctttaaagactacgctgaagctcatgctaaactgagcgaccttggtgcaaagttcgatccacctgaggtgaggactaccatctttttttttcattttgatctcctggcaaccaattgtgcctaaacaatcataaacaatacgaaagacacttaagctcttaagttcttttattagaacatgccagattttcttcctcttgtttgcaagttcaaaacatgactccctgattcctcgtccacatcgagtagatatcttttgtaatgtattttttttctagagaattcagtaatgtacttatgtgacagtaagatggagtactggaccttcaggacagaaatatagttcagatagtttttctttttaccgaatgtaatccaaacactgggagtttgaggtagtccatcatatcaatctttcttctgcaatgcaacgaaatggggtttactatggcagcttttcttagctgttcttcatgtaaaaaccagtgcaattgtaggttggatatttacagagtccaactttaccagccttcgatcaggaagtgatggatgtgattttcctgcagggattttcactggacgatgaaccagccgtcgaagagaaggatcctgaaccagcaccagcgccagcagcagcaccaccacctccaccagtcgaggagaagaaggaagctgaaccaactccagtaccagtaacggtaggagcagcagtggcatcatcgccagcggatgacaacaacggtgcagcaccgcaaccagagcccttcgtcgctgcgaaatactcctacggaaaggtatgcactctccacgaagcctagcttctagccctagatttgatggacaatgcatggtatcttgcaatggcttttgcagaaggagctgtcggactcgatgaagcagaagatcagggcggagtacgagggattcggaggcagcccggacaagcctctgcagtccaactacttcctcaacatcatgctcttgatcggagggctggccttcttgacgtctctgctcgggagctgagagcgatggtctgatgacctcctctgacgagtgttttgagttgttctgcctgtgctaagatttgcgtgtttctctttccatgttttgagtcgttattccgtaaataaattgaggtaaaaggatgggcatgtgaatggattccagtactttctgaacttcttgagtaattcctctagagaaatatttgtcggagagaaatgtcacattatctagttgtcatggctcatgact</dnaseqindica>

External Link(s)

NCBI Gene:Os02g0553200, RefSeq:Os02g0553200

  1. 1.0 1.1 1.2 1.3 1.4 Chwan-Yang Hong and Ching Huei Kao. NaCl-induced expression of ASCORBATE PEROXIDASE 8 in roots of rice(Oryza sativa L.)seedlings is not associated with osmotic component[J]. Plant Signaling & Behavior, 2008, 3(3): 199-201.
  2. 2.00 2.01 2.02 2.03 2.04 2.05 2.06 2.07 2.08 2.09 2.10 2.11 2.12 Chwan-Yang Hong, Yi Ting Hsu, Yu-Chang Tsai, et al. Expression of ASCORBATE PEROXIDASE 8 in roots of rice (Oryza sativa L.)seedlings in response to NaCl [J]. Journal of Experimental Botany, 2007, 58(12): 3273-3283.
  3. 3.0 3.1 3.2 3.3 Chwan-Yang Hong, Yun-Yang Chao, Min-Yu Yang, et al. NaCl-induced expression of glutathione reductase in roots of rice (Oryza sativa L.) seedlings is mediated through hydrogen peroxide but not abscisic acid[J]. Plant Soil, 2009, 320: 103-115.
  4. 4.0 4.1 Ting-Shao Chou, Yun-Yang Chao and Ching Huei Kao. Involvement of hydrogen peroxide in heat shock- and cadmium-induced expression of ascorbate peroxidase and glutathione reductase in leaves of rice seedlings. Journal of Plant Physiology, 2012, 169: 478-486.
  5. 5.0 5.1 5.2 5.3 5.4 5.5 Andréia Caverzana, Aurenivia Bonifaciod, Fabricio E.L. Carvalhod, et al. The knockdown of chloroplastic ascorbate peroxidases reveals itsregulatory role in the photosynthesis and protection underphoto-oxidative stress in rice. Plant Science, 2014, 214: 74-87.
  6. 6.0 6.1 Cite error: Invalid <ref> tag; no text was provided for refs named ref6