tailieunhanh - Báo cáo khoa học: Barley polyamine oxidase isoforms 1 and 2, a peculiar case of gene duplication

Polyamine oxidases (PAOs, EC ) are key enzymes responsible for the terminal catabolism of polyamines in plants, bacteria and protozoa. In barley, two PAO isoforms (HvPAO1 and HvPAO2) have been previously analyzed as regards their tissue expression and subcellular localization. | ễFEBS Journal Barley polyamine oxidase isoforms 1 and 2 a peculiar case of gene duplication Manuela Cervelli1 Marzia Bianchi1 Alessandra Cona1 Cristina Crosatti2 Michele Stanca2 Riccardo Angelini1 Rodolfo Federico1 and Paolo Mariottini1 1 Dipartimento di Biologia Universita Roma Tre Rome Italy 2 Istituto Sperimentale per la Cerealicoltura Sezione di Fiorenzuola d Arda PC Italy Keywords biochemical characterization enzyme isoform gene duplication polyamine oxidase tissue specificity Correspondence P. Mariottini Dipartimento di Biologia University degli Studi Roma Tre Viale Guglielmo Marconi 446 00146 Roma Italy Fax 39 06 55176321 Tel 39 06 55176359 E-mail mariotpa@ Received 09 May 2006 revised 23 June 2006 accepted 30 June 2006 doi Polyamine oxidases PAOs EC are key enzymes responsible for the terminal catabolism of polyamines in plants bacteria and protozoa. In barley two PAO isoforms HvPAO1 and HvPAO2 have been previously analyzed as regards their tissue expression and subcellular localization. Only the major isoform HvPAO2 has been biochemically characterized up to now. In order to study the ear-specific expression of the HvPAO1 isoform in detail RT-PCR analysis was performed in barley on the whole ear and on various ear tissues. Moreover HvPAO1promoter GUS transient expression was examined in barley developing caryopses at 30-day postfertilization. Results from these analyses have demonstrated that the HvPAO1 gene is specifically expressed in all the ear organs analyzed . basal lemma rachis awn embryo-deprived caryopsis embryo and sterile spikelets at variance with the HvPAO2 gene which is expressed at high levels in sterile spikelets and at very low levels in embryos. We purified HvPAO1 from barley immature caryopses and characterized its catalytic properties. Furthermore we carried out in vitro synthesis of HvPAO1 protein in a cell-free translation system. The HvPAO1 enzymes purified from immature .

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