Among other enzymes, peroxidases have been proposed to participate in the latest steps of lignin biosynthesis. In order to identify new proteins involved in such mechanism of lignification in maize, we have isolated three cDNAs coding for three different peroxidases, named ZmPox1, ZmPox2, and ZmPox3, respectively. Computational analyses of these three proteins correlate with features typically attributed to heme-containing plant peroxidases of approximately 300 amino acid residues. Although with different expression levels, ZmPox2 and ZmPox3 mRNAs are accumulated in the elongating region of young roots but not in the root tips. In addition, the ZmPox2 mRNA levels are up-regulated by wounding and ethylene treatments. However, ZmPox1 is also expressed in the root tip meristems, where lignification does not occur. Finally, in situ hybridisations indicate that ZmPox2 mRNA localises in vascular tissues and epidermis. Although ZmPox1 mRNA localises in the same regions as ZmPox2 mRNA in root tips, its mRNA is only detected in the epidermis but not in the vascular tissues of young roots, suggesting that the function of ZmPox1 is not correlated to lignification. In addition, although ZmPox3 mRNA is also detected in the regions where lignification occurs, the involvement of this peroxidase in such a mechanism remains to be further investigated due to its very low expression level. Therefore, based on its amino acid sequence and mRNA accumulation and localisation patterns, the involvement of ZmPox2 in the latest steps of lignification is discussed.
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http://purl.uniprot.org/cit... | rdfs:comment | Among other enzymes, peroxidases have been proposed to participate in the latest steps of lignin biosynthesis. In order to identify new proteins involved in such mechanism of lignification in maize, we have isolated three cDNAs coding for three different peroxidases, named ZmPox1, ZmPox2, and ZmPox3, respectively. Computational analyses of these three proteins correlate with features typically attributed to heme-containing plant peroxidases of approximately 300 amino acid residues. Although with different expression levels, ZmPox2 and ZmPox3 mRNAs are accumulated in the elongating region of young roots but not in the root tips. In addition, the ZmPox2 mRNA levels are up-regulated by wounding and ethylene treatments. However, ZmPox1 is also expressed in the root tip meristems, where lignification does not occur. Finally, in situ hybridisations indicate that ZmPox2 mRNA localises in vascular tissues and epidermis. Although ZmPox1 mRNA localises in the same regions as ZmPox2 mRNA in root tips, its mRNA is only detected in the epidermis but not in the vascular tissues of young roots, suggesting that the function of ZmPox1 is not correlated to lignification. In addition, although ZmPox3 mRNA is also detected in the regions where lignification occurs, the involvement of this peroxidase in such a mechanism remains to be further investigated due to its very low expression level. Therefore, based on its amino acid sequence and mRNA accumulation and localisation patterns, the involvement of ZmPox2 in the latest steps of lignification is discussed. | lld:uniprot |
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http://purl.uniprot.org/cit... | uniprot:name | Gene | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:author | Puigdomenech P. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:author | Rigau J. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:author | Vignols F. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:author | Caparros-Ruiz D. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:author | de Obeso M. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:date | 2003 | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:pages | 23-33 | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:title | Characterisation of maize peroxidases having differential patterns of mRNA accumulation in relation to lignifying tissues. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:volume | 309 | lld:uniprot |
http://purl.uniprot.org/cit... | dc-term:identifier | doi:10.1016/S0378-1119(03)00462-1 | lld:uniprot |
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