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Nat Commun. 2014 Aug 5;5:4572. doi: 10.1038/ncomms5572.

O-GlcNAc-mediated interaction between VER2 and TaGRP2 elicits TaVRN1 mRNA accumulation during vernalization in winter wheat.

Author information

1
1] Key Laboratory of Plant Molecular Physiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China [2] University of the Chinese Academy of Sciences, Beijing 100049, China [3].
2
Key Laboratory of Plant Molecular Physiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
3
1] Key Laboratory of Plant Molecular Physiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China [2] University of the Chinese Academy of Sciences, Beijing 100049, China.
4
Hybrid Wheat Research Center, Beijing Academy of Agriculture and Forestry Sciences, Beijing 100089, China.
5
Department of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
6
Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China.
7
1] Key Laboratory of Plant Molecular Physiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China [2] National Center for Plant Gene Research, Beijing 100093, China.

Abstract

Vernalization, sensing of prolonged cold, is important for seasonal flowering in eudicots and monocots. While vernalization silences a repressor (FLC, MADS-box transcription factor) in eudicots, it induces an activator (TaVRN1, an AP1 clade MADS-box transcription factor) in monocots. The mechanism for TaVRN1 induction during vernalization is not well understood. Here we reveal a novel mechanism for controlling TaVRN1 mRNA accumulation in response to prolonged cold sensing in wheat. The carbohydrate-binding protein VER2, a jacalin lectin, promotes TaVRN1 upregulation by physically interacting with the RNA-binding protein TaGRP2. TaGRP2 binds to TaVRN1 pre-mRNA and inhibits TaVRN1 mRNA accumulation. The physical interaction between VER2 and TaGRP2 is controlled by TaGRP2 O-GlcNAc modification, which gradually increases during vernalization. The interaction between VER2 and O-GlcNAc-TaGRP2 reduces TaGRP2 protein accumulation in the nucleus and/or promotes TaGRP2 dissociation from TaVRN1, leading to TaVRN1 mRNA accumulation. Our data reveal a new mechanism for sensing prolonged cold in temperate cereals.

PMID:
25091017
PMCID:
PMC4143922
DOI:
10.1038/ncomms5572
[Indexed for MEDLINE]
Free PMC Article

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