A plant spermine oxidase/dehydrogenase regulated by the proteasome and polyamines

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 differences in primary structure, substrate specificity, subcellular localization,...

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Veröffentlicht in:Journal of experimental botany. - 1985. - 65(2014), 6 vom: 18. Apr., Seite 1585-603
1. Verfasser: Ahou, Abdellah (VerfasserIn)
Weitere Verfasser: Martignago, Damiano, Alabdallah, Osama, Tavazza, Raffaela, Stano, Pasquale, Macone, Alberto, Pivato, Micaela, Masi, Antonio, Rambla, Jose L, Vera-Sirera, Francisco, Angelini, Riccardo, Federico, Rodolfo, Tavladoraki, Paraskevi
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2014
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Acetylated polyamines dehydrogenase polyamine oxidase polyamines spermidine spermine thermospermine. Polyamines mehr... Recombinant Fusion Proteins Oxidoreductases Acting on CH-NH Group Donors EC 1.5.- Proteasome Endopeptidase Complex EC 3.4.25.1
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100 1 |a Ahou, Abdellah  |e verfasserin  |4 aut 
245 1 2 |a A plant spermine oxidase/dehydrogenase regulated by the proteasome and polyamines 
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520 |a 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 differences 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 uncharacterized AtPAO which is specifically expressed in the vascular system, was partially purified from 35S::AtPAO5-6His Arabidopsis transgenic plants and biochemically characterized. Data presented here allow AtPAO5 to be classified as a spermine dehydrogenase. It is also shown that AtPAO5 oxidizes the polyamines spermine, thermospermine, and N(1)-acetylspermine, the latter being the best in vitro substrate of the recombinant enzyme. AtPAO5 also oxidizes these polyamines in vivo, as was evidenced by analysis of polyamine levels in the 35S::AtPAO5-6His Arabidopsis transgenic plants, as well as in a loss-of-function atpao5 mutant. Furthermore, subcellular localization studies indicate that AtPAO5 is a cytosolic protein undergoing proteasomal control. Positive regulation of AtPAO5 expression by polyamines at the transcriptional and post-transcriptional level is also shown. These data provide new insights into the catalytic properties of the PAO gene family and the complex regulatory network controlling polyamine metabolism 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Acetylated polyamines 
650 4 |a dehydrogenase 
650 4 |a polyamine oxidase 
650 4 |a polyamines 
650 4 |a spermidine 
650 4 |a spermine 
650 4 |a thermospermine. 
650 7 |a Polyamines  |2 NLM 
650 7 |a Recombinant Fusion Proteins  |2 NLM 
650 7 |a Oxidoreductases Acting on CH-NH Group Donors  |2 NLM 
650 7 |a EC 1.5.-  |2 NLM 
650 7 |a Proteasome Endopeptidase Complex  |2 NLM 
650 7 |a EC 3.4.25.1  |2 NLM 
700 1 |a Martignago, Damiano  |e verfasserin  |4 aut 
700 1 |a Alabdallah, Osama  |e verfasserin  |4 aut 
700 1 |a Tavazza, Raffaela  |e verfasserin  |4 aut 
700 1 |a Stano, Pasquale  |e verfasserin  |4 aut 
700 1 |a Macone, Alberto  |e verfasserin  |4 aut 
700 1 |a Pivato, Micaela  |e verfasserin  |4 aut 
700 1 |a Masi, Antonio  |e verfasserin  |4 aut 
700 1 |a Rambla, Jose L  |e verfasserin  |4 aut 
700 1 |a Vera-Sirera, Francisco  |e verfasserin  |4 aut 
700 1 |a Angelini, Riccardo  |e verfasserin  |4 aut 
700 1 |a Federico, Rodolfo  |e verfasserin  |4 aut 
700 1 |a Tavladoraki, Paraskevi  |e verfasserin  |4 aut 
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773 1 8 |g volume:65  |g year:2014  |g number:6  |g day:18  |g month:04  |g pages:1585-603 
856 4 0 |u http://dx.doi.org/10.1093/jxb/eru016  |3 Volltext 
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