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A Polyamine Oxidase from Selaginella lepidophylla (SelPAO5) can Replace AtPAO5 in Arabidopsis through Converting Thermospermine to Norspermidine instead to Spermidine.


ABSTRACT: Of the five polyamine oxidases in Arabidopsis thaliana, AtPAO5 has a substrate preference for the tetraamine thermospermine (T-Spm) which is converted to triamine spermidine (Spd) in a back-conversion reaction in vitro. A homologue of AtPAO5 from the lycophyte Selaginella lepidophylla (SelPAO5) back-converts T-Spm to the uncommon polyamine norspermidine (NorSpd) instead of Spd. An Atpao5 loss-of-function mutant shows a strong reduced growth phenotype when growing on a T-Spm containing medium. When SelPAO5 was expressed in the Atpao5 mutant, T-Spm level decreased to almost normal values of wild type plants, and NorSpd was produced. Furthermore the reduced growth phenotype was cured by the expression of SelPAO5. Thus, a NorSpd synthesis pathway by PAO reaction and T-Spm as substrate was demonstrated in planta and the assumption that a balanced T-Spm homeostasis is needed for normal growth was strengthened.

SUBMITTER: Sagor GHM 

PROVIDER: S-EPMC6524367 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature

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A Polyamine Oxidase from <i>Selaginella lepidophylla</i> (SelPAO5) can Replace AtPAO5 in <i>Arabidopsis</i> through Converting Thermospermine to Norspermidine instead to Spermidine.

Sagor G H M GHM   Kusano Tomonobu T   Berberich Thomas T  

Plants (Basel, Switzerland) 20190415 4


Of the five polyamine oxidases in <i>Arabidopsis thaliana</i>, AtPAO5 has a substrate preference for the tetraamine thermospermine (T-Spm) which is converted to triamine spermidine (Spd) in a back-conversion reaction in vitro. A homologue of AtPAO5 from the lycophyte <i>Selaginella lepidophylla</i> (SelPAO5) back-converts T-Spm to the uncommon polyamine norspermidine (NorSpd) instead of Spd. An <i>Atpao5</i> loss-of-function mutant shows a strong reduced growth phenotype when growing on a T-Spm  ...[more]

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