Journal of Experimental Botany, Vol. 65, No. 6, pp. 1585–1603, 2014 doi:10.1093/jxb/eru016 Advance Access publication 18 February, 2014 RESEARCH PAPER A plant spermine oxidase/dehydrogenase regulated by the proteasome and polyamines Downloaded from https://academic.oup.com/jxb/article-abstract/65/6/1585/588180 by Divisione Coordinamento Biblioteche MI user on 10 June 2020 Abdellah Ahou1, Damiano Martignago1, Osama Alabdallah1, Raffaela Tavazza2, Pasquale Stano1, Alberto Macone3, Micaela Pivato4,5, Antonio Masi4, Jose L. Rambla6, Francisco Vera-Sirera6, Riccardo Angelini1, Rodolfo Federico1 and Paraskevi Tavladoraki1,* 1 Department of Science, University ‘ROMA TRE’, Rome, Italy 2 Italian National Agency for New Technologies, Energy and Sustainable Economic Development (ENEA), UTAGRI-INN C.R. Casaccia, Rome, Italy 3 Department of Biochemical Sciences ‘A. Rossi Fanelli’, University ‘La Sapienza’, Rome, Italy 4 DAFNAE, University of Padova, Legnaro, Italy 5 Proteomics Center of Padova University, Padova, Italy 6 Instituto de Biología Molecular y Celular de Plantas, UPV-CSIC, Valencia, Spain * To whom correspondence should be addressed. E-mail:
[email protected] Received 31 October 2013; Revised 20 December 2013; Accepted 7 January 2014 Abstract Polyamine oxidases (PAOs) are flavin-dependent enzymes involved in polyamine catabolism. In Arabidopsis five PAO genes (AtPAO1–AtPAO5) have been identified which present some common characteristics, but also important dif- ferences in primary structure, substrate specificity, subcellular localization, and tissue-specific expression pattern, differences which may suggest distinct physiological roles. In the present work, AtPAO5, the only so far uncharac- terized AtPAO which is specifically expressed in the vascular system, was partially purified from 35S::AtPAO5-6His Arabidopsis transgenic plants and biochemically characterized.