Recycling of pyridoxine (vitamin B6) by PUP1 in Arabidopsis. (16th May 2013)
- Record Type:
- Journal Article
- Title:
- Recycling of pyridoxine (vitamin B6) by PUP1 in Arabidopsis. (16th May 2013)
- Main Title:
- Recycling of pyridoxine (vitamin B6) by PUP1 in Arabidopsis
- Authors:
- Szydlowski, Nicolas
Bürkle, Lukas
Pourcel, Lucille
Moulin, Michael
Stolz, Jürgen
Fitzpatrick, Teresa B. - Abstract:
- Summary: Vitamin B6 is a cofactor for more than 140 essential enzymatic reactions and was recently proposed as a potent antioxidant, playing a role in the photoprotection of plants. De novo biosynthesis of the vitamin has been described relatively recently and is derived from simple sugar precursors as well as glutamine. In addition, the vitamin can be taken up from exogenous sources in a broad range of organisms, including plants. However, specific transporters have been identified only in yeast. Here we assess the ability of the family of Arabidopsis purine permeases (PUPs) to transport vitamin B6. Several members of the family complement the growth phenotype of a Saccharomyces cerevisiae mutant strain impaired in both de novo biosynthesis of vitamin B6 as well as its uptake. The strongest activity was observed with PUP1 and was confirmed by direct measurement of uptake in yeast as well as in planta, defining PUP1 as a high affinity transporter for pyridoxine. At the tissue level the protein is localised to hydathodes and here we use confocal microscopy to illustrate that at the cellular level it is targeted to the plasma membrane. Interestingly, we observe alterations in pyridoxine recycling from the guttation sap upon overexpression of PUP1 and in a pup1 mutant, consistent with the role of the protein in retrieval of pyridoxine. Furthermore, combining the pup1 mutant with a vitamin B6 de novo biosynthesis mutant ( pdx1.3 ) corroborates that PUP1 is involved in the uptakeSummary: Vitamin B6 is a cofactor for more than 140 essential enzymatic reactions and was recently proposed as a potent antioxidant, playing a role in the photoprotection of plants. De novo biosynthesis of the vitamin has been described relatively recently and is derived from simple sugar precursors as well as glutamine. In addition, the vitamin can be taken up from exogenous sources in a broad range of organisms, including plants. However, specific transporters have been identified only in yeast. Here we assess the ability of the family of Arabidopsis purine permeases (PUPs) to transport vitamin B6. Several members of the family complement the growth phenotype of a Saccharomyces cerevisiae mutant strain impaired in both de novo biosynthesis of vitamin B6 as well as its uptake. The strongest activity was observed with PUP1 and was confirmed by direct measurement of uptake in yeast as well as in planta, defining PUP1 as a high affinity transporter for pyridoxine. At the tissue level the protein is localised to hydathodes and here we use confocal microscopy to illustrate that at the cellular level it is targeted to the plasma membrane. Interestingly, we observe alterations in pyridoxine recycling from the guttation sap upon overexpression of PUP1 and in a pup1 mutant, consistent with the role of the protein in retrieval of pyridoxine. Furthermore, combining the pup1 mutant with a vitamin B6 de novo biosynthesis mutant ( pdx1.3 ) corroborates that PUP1 is involved in the uptake of the vitamin. … (more)
- Is Part Of:
- Plant journal. Volume 75:Number 1(2013:Jul.)
- Journal:
- Plant journal
- Issue:
- Volume 75:Number 1(2013:Jul.)
- Issue Display:
- Volume 75, Issue 1 (2013)
- Year:
- 2013
- Volume:
- 75
- Issue:
- 1
- Issue Sort Value:
- 2013-0075-0001-0000
- Page Start:
- 40
- Page End:
- 52
- Publication Date:
- 2013-05-16
- Subjects:
- vitamin B6 -- transport -- PUP proteins -- cytokinins -- recycling -- Arabidopsis
Plant molecular biology -- Periodicals
Plant cells and tissues -- Periodicals
Botany -- Periodicals
580 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-313X ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/tpj.12195 ↗
- Languages:
- English
- ISSNs:
- 0960-7412
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6519.200000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 8734.xml