Cytochrome P450 superfamily (CYP) is a large and diverse group of heme proteins able to catalyse the oxidation of organic substances by reducing oxygen to water (using NADH or NADPH). CYP proteins are object of particular interest for chemical and pharmaceutical companies, due to their potential to overcome the constraints of chemical synthesis. In plants, CYP82 family lacks orthologs in rice genome and might be a family evolved only in dicots. CYP82E4 from tobacco is a nicotine N-demethylase, that is responsible for conversion of nicotine to nornicotine and 8-methoxypsoralen is a substrate for CYP82C4; however the in vivo functions of Arabidopsis CYP82 family members are currently unknown. CYP82C4 (At4g31940) was identified as one of the genes highly expressed in Fe-deficient Arabidopsis thaliana roots, together with 2 other CYP genes, i.e. CYP82C3 (At4g31950) and CYP71B5 (At3g53280). By performing expression correlation analysis we show that, differently from CYP82C3 and CYP71B5, CYP82C4 is specifically correlated with genes involved in metal uptake and transport. Moreover, CYP82C4 promoter region possesses both IDE1-like and RY sequences, supporting CYP82C4 specific involvement in the Fe-deficiency response. We confirmed that CYP82C4 transcript accumulates in seedlings under Fe-deficient conditions whereas, in Fe-sufficient conditions, its level fluctuates during the day. For investigating its role in the Fe deficiency response, we isolated Arabidopsis cyp82c4-1 mutant, KO for CYP82C4 gene and a preliminary characterization of such mutant will be given.

Cytochrome P450 CYP82C4 correlates with genes involved in the metal uptake and transport in Arabidopsis thaliana / I. Murgia, D. Tarantino, P. Morandini, F. Paieri, C. Soave. ((Intervento presentato al convegno International Symposium on iron nutrition and interactions in plants tenutosi a Budapest nel 2010.

Cytochrome P450 CYP82C4 correlates with genes involved in the metal uptake and transport in Arabidopsis thaliana

I. Murgia
Primo
;
D. Tarantino
Secondo
;
P. Morandini;C. Soave
Ultimo
2010

Abstract

Cytochrome P450 superfamily (CYP) is a large and diverse group of heme proteins able to catalyse the oxidation of organic substances by reducing oxygen to water (using NADH or NADPH). CYP proteins are object of particular interest for chemical and pharmaceutical companies, due to their potential to overcome the constraints of chemical synthesis. In plants, CYP82 family lacks orthologs in rice genome and might be a family evolved only in dicots. CYP82E4 from tobacco is a nicotine N-demethylase, that is responsible for conversion of nicotine to nornicotine and 8-methoxypsoralen is a substrate for CYP82C4; however the in vivo functions of Arabidopsis CYP82 family members are currently unknown. CYP82C4 (At4g31940) was identified as one of the genes highly expressed in Fe-deficient Arabidopsis thaliana roots, together with 2 other CYP genes, i.e. CYP82C3 (At4g31950) and CYP71B5 (At3g53280). By performing expression correlation analysis we show that, differently from CYP82C3 and CYP71B5, CYP82C4 is specifically correlated with genes involved in metal uptake and transport. Moreover, CYP82C4 promoter region possesses both IDE1-like and RY sequences, supporting CYP82C4 specific involvement in the Fe-deficiency response. We confirmed that CYP82C4 transcript accumulates in seedlings under Fe-deficient conditions whereas, in Fe-sufficient conditions, its level fluctuates during the day. For investigating its role in the Fe deficiency response, we isolated Arabidopsis cyp82c4-1 mutant, KO for CYP82C4 gene and a preliminary characterization of such mutant will be given.
giu-2010
Settore BIO/04 - Fisiologia Vegetale
Settore AGR/13 - Chimica Agraria
Settore BIO/11 - Biologia Molecolare
Cytochrome P450 CYP82C4 correlates with genes involved in the metal uptake and transport in Arabidopsis thaliana / I. Murgia, D. Tarantino, P. Morandini, F. Paieri, C. Soave. ((Intervento presentato al convegno International Symposium on iron nutrition and interactions in plants tenutosi a Budapest nel 2010.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/213276
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