Molecular Analysis of Class III Peroxidases from Cotton
نویسندگان
چکیده
A molecular analysis of class III peroxidases from cotton (Gossypium hirsutum L.) was undertaken using the sequence of 12 genes available in databanks. Sequence comparison, phylogenetical analysis, and investigation of expression in organs were performed to characterize this group of peroxidases in cotton. All 12 genes possess the characteristics of class III peroxidases, including three conserved domains with the catalytic histidines involved in haem-binding and catalysis, four disulfide bridges, a salt bridge, a signal peptide that targets the protein to the secretory pathway, and putative N-glycosylation sites. Possible functions for these peroxidases according to their phylogenetical position and the existence of close orthologs in other plant families are suggested. Two class III peroxidases from cotton play a role in the oxidative burst response of cotton to bacterial blight.
منابع مشابه
The role of xylem class III peroxidases in lignification.
Lignification is a cell wall fortifying process which occurs in xylem tissue in a scheduled manner during tissue differentiation. In this review, enzymes and the genes responsible for lignin biosynthesis have been studied with an emphasis on lignin polymerizing class III secretable plant peroxidases. Our aim is to understand the cell and molecular biology of the polymerization of lignin especia...
متن کاملMembrane-bound guaiacol peroxidases from maize (Zea mays L.) roots are regulated by methyl jasmonate, salicylic acid, and pathogen elicitors
Plant peroxidases are involved in numerous cellular processes in plant development and stress responses. Four plasma membrane-bound peroxidases have been identified and characterized in maize (Zea mays L.) roots. In the present study, maize seedlings were treated with different stresses and signal compounds, and a functional analysis of these membrane-bound class III peroxidases (pmPOX1, pmPOX2...
متن کاملThree differentially expressed basic peroxidases from wound-lignifying Asparagus officinalis.
The activity of ionically bound peroxidases from an asparagus spear increased from 5-24 h post-harvest. Isoelectric focusing showed that the post-harvest increase of the total peroxidase activity was due to the increase of several distinct isoperoxidases. Concomitantly, a decrease in the activity of two anionic peroxidases was observed. Peroxidases with pI 5.9, 6.4 and 9.2 were detected only at...
متن کاملPurification and characterization of a novel class III peroxidase isoenzyme from tea leaves.
A novel, basic (isoelectric point > 10), heme peroxidase isoenzyme (TP; relative molecular weight = 34,660 +/- 10, mean +/- SE) that can account for a significant part of the ascorbate peroxidase activity in tea (Camellia sinensis) leaves has been purified to homogeneity. The ultraviolet/visible absorption spectrum is typical of heme-containing plant peroxidases, with a Soret peak at 406 nm (ep...
متن کاملSpecific functions of individual class III peroxidase genes.
In higher plants, class III peroxidases exist as large multigene families (e.g. 73 genes in Arabidopsis thaliana). The diversity of processes catalysed by peroxidases as well as the large number of their genes suggests the possibility of a functional specialization of each isoform. In addition, the fact that peroxidase promoter sequences are very divergent and that protein sequences contain bot...
متن کامل