Cargando…

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

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Sagor, G. H. M., Kusano, Tomonobu, Berberich, Thomas
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6524367/
https://www.ncbi.nlm.nih.gov/pubmed/30991762
http://dx.doi.org/10.3390/plants8040099
_version_ 1783419546548305920
author Sagor, G. H. M.
Kusano, Tomonobu
Berberich, Thomas
author_facet Sagor, G. H. M.
Kusano, Tomonobu
Berberich, Thomas
author_sort Sagor, G. H. M.
collection PubMed
description 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.
format Online
Article
Text
id pubmed-6524367
institution National Center for Biotechnology Information
language English
publishDate 2019
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-65243672019-06-05 A Polyamine Oxidase from Selaginella lepidophylla (SelPAO5) can Replace AtPAO5 in Arabidopsis through Converting Thermospermine to Norspermidine instead to Spermidine Sagor, G. H. M. Kusano, Tomonobu Berberich, Thomas Plants (Basel) Article 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. MDPI 2019-04-15 /pmc/articles/PMC6524367/ /pubmed/30991762 http://dx.doi.org/10.3390/plants8040099 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Sagor, G. H. M.
Kusano, Tomonobu
Berberich, Thomas
A Polyamine Oxidase from Selaginella lepidophylla (SelPAO5) can Replace AtPAO5 in Arabidopsis through Converting Thermospermine to Norspermidine instead to Spermidine
title A Polyamine Oxidase from Selaginella lepidophylla (SelPAO5) can Replace AtPAO5 in Arabidopsis through Converting Thermospermine to Norspermidine instead to Spermidine
title_full A Polyamine Oxidase from Selaginella lepidophylla (SelPAO5) can Replace AtPAO5 in Arabidopsis through Converting Thermospermine to Norspermidine instead to Spermidine
title_fullStr A Polyamine Oxidase from Selaginella lepidophylla (SelPAO5) can Replace AtPAO5 in Arabidopsis through Converting Thermospermine to Norspermidine instead to Spermidine
title_full_unstemmed A Polyamine Oxidase from Selaginella lepidophylla (SelPAO5) can Replace AtPAO5 in Arabidopsis through Converting Thermospermine to Norspermidine instead to Spermidine
title_short A Polyamine Oxidase from Selaginella lepidophylla (SelPAO5) can Replace AtPAO5 in Arabidopsis through Converting Thermospermine to Norspermidine instead to Spermidine
title_sort polyamine oxidase from selaginella lepidophylla (selpao5) can replace atpao5 in arabidopsis through converting thermospermine to norspermidine instead to spermidine
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6524367/
https://www.ncbi.nlm.nih.gov/pubmed/30991762
http://dx.doi.org/10.3390/plants8040099
work_keys_str_mv AT sagorghm apolyamineoxidasefromselaginellalepidophyllaselpao5canreplaceatpao5inarabidopsisthroughconvertingthermosperminetonorspermidineinsteadtospermidine
AT kusanotomonobu apolyamineoxidasefromselaginellalepidophyllaselpao5canreplaceatpao5inarabidopsisthroughconvertingthermosperminetonorspermidineinsteadtospermidine
AT berberichthomas apolyamineoxidasefromselaginellalepidophyllaselpao5canreplaceatpao5inarabidopsisthroughconvertingthermosperminetonorspermidineinsteadtospermidine
AT sagorghm polyamineoxidasefromselaginellalepidophyllaselpao5canreplaceatpao5inarabidopsisthroughconvertingthermosperminetonorspermidineinsteadtospermidine
AT kusanotomonobu polyamineoxidasefromselaginellalepidophyllaselpao5canreplaceatpao5inarabidopsisthroughconvertingthermosperminetonorspermidineinsteadtospermidine
AT berberichthomas polyamineoxidasefromselaginellalepidophyllaselpao5canreplaceatpao5inarabidopsisthroughconvertingthermosperminetonorspermidineinsteadtospermidine