PUMPKIN, the Sole Plastid UMP Kinase, Associates with Group II Introns and Alters Their Metabolism

The chloroplast hosts photosynthesis and a variety of metabolic pathways that are essential for plant viability and acclimation processes. In this study, we show that the sole plastid UMP kinase (PUMPKIN) in Arabidopsis ( ) associates specifically with the introns of the plastid transcripts -UCC, -U...

Full description

Saved in:
Bibliographic Details
Published in:Plant physiology (Bethesda) 2019-01, Vol.179 (1), p.248-264
Main Authors: Schmid, Lisa-Marie, Ohler, Lisa, Möhlmann, Torsten, Brachmann, Andreas, Muiño, Jose M, Leister, Dario, Meurer, Jörg, Manavski, Nikolay
Format: Article
Language:English
Subjects:
Arabidopsis - enzymology
Arabidopsis - genetics
Arabidopsis - physiology
Arabidopsis Proteins - physiology
Gene Expression Regulation, Plant
Genes, Plant
Introns - genetics
Nucleoside-Phosphate Kinase - physiology
Photosynthesis
Plastids - enzymology
Plastids - metabolism
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The chloroplast hosts photosynthesis and a variety of metabolic pathways that are essential for plant viability and acclimation processes. In this study, we show that the sole plastid UMP kinase (PUMPKIN) in Arabidopsis ( ) associates specifically with the introns of the plastid transcripts -UCC, -UAC, and in vivo, as revealed by RNA immunoprecipitation coupled with deep sequencing (RIP-Seq); and that PUMPKIN can bind RNA efficiently in vitro. Analyses of target transcripts showed that PUMPKIN affects their metabolism. Null alleles and knockdowns of were viable but clearly affected in growth, plastid translation, and photosynthetic performance. In mutants, the levels of many plastid transcripts were reduced, while the amounts of others were increased, as revealed by RNA-Seq analysis. PUMPKIN is a homomultimeric, plastid-localized protein that forms in vivo RNA-containing megadalton-sized complexes and catalyzes the ATP-dependent conversion of UMP to UDP in vitro with properties characteristic of known essential eubacterial UMP kinases. A moonlighting function of PUMPKIN combining RNA and pyrimidine metabolism is discussed.
ISSN:0032-0889
1532-2548
DOI:10.1104/pp.18.00687