PAPST2 Plays Critical Roles in Removing the Stress Signaling Molecule 3'-Phosphoadenosine 5'-Phosphate from the Cytosol and Its Subsequent Degradation in Plastids and Mitochondria.
Journal
The Plant cell
ISSN: 1532-298X
Titre abrégé: Plant Cell
Pays: England
ID NLM: 9208688
Informations de publication
Date de publication:
01 2019
01 2019
Historique:
received:
06
07
2018
revised:
15
10
2018
accepted:
15
11
2018
pubmed:
23
11
2018
medline:
6
2
2020
entrez:
23
11
2018
Statut:
ppublish
Résumé
The compartmentalization of PAPS (the sulfate donor 3'-phosphoadenosine 5'-phosphosulfate) synthesis (mainly in plastids), PAPS consumption (in the cytosol), and PAP (the stress signaling molecule 3'-phosphoadenosine 5'-phosphate) degradation (in plastids and mitochondria) requires organellar transport systems for both PAPS and PAP. The plastidial transporter PAPST1 (PAPS TRANSPORTER1) delivers newly synthesized PAPS from the stroma to the cytosol. We investigated the activity of PAPST2, the closest homolog of PAPST1, which unlike PAPST1 is targeted to both the plastids and mitochondria. Biochemical characterization in
Identifiants
pubmed: 30464037
pii: tpc.18.00512
doi: 10.1105/tpc.18.00512
pmc: PMC6391701
doi:
Substances chimiques
Membrane Transport Proteins
0
Adenosine Diphosphate
61D2G4IYVH
adenosine 3'-phosphate-5'-phosphate
C65F80D52U
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
231-249Commentaires et corrections
Type : CommentIn
Informations de copyright
© 2018 American Society of Plant Biologists. All rights reserved.
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