Factorial combinations of protein interactions generate a multiplicity of florigen activation complexes in wheat and barley. (6th September 2015)
- Record Type:
- Journal Article
- Title:
- Factorial combinations of protein interactions generate a multiplicity of florigen activation complexes in wheat and barley. (6th September 2015)
- Main Title:
- Factorial combinations of protein interactions generate a multiplicity of florigen activation complexes in wheat and barley
- Authors:
- Li, Chengxia
Lin, Huiqiong
Dubcovsky, Jorge - Abstract:
- <abstract abstract-type="main" id="tpj12960-abs-0001"> <title>Summary</title> <p>The FLOWERING LOCUS T (FT) protein is a central component of a mobile flowering signal (florigen) that is transported from leaves to the shoot apical meristem (SAM). Two FT monomers and two DNA‐binding bZIP transcription factors interact with a dimeric 14‐3‐3 protein bridge to form a hexameric protein complex. This complex, designated as the 'florigen activation complex' (FAC), plays a critical role in flowering. The wheat homologue of FT, designated FT1 (= VRN3), activates expression of <italic>VRN1</italic> in the leaves and the SAM, promoting flowering under inductive long days. In this study, we show that FT1, other FT‐like proteins, and different FD‐like proteins, can interact with multiple wheat and barley 14‐3‐3 proteins. We also identify the critical amino acid residues in FT1 and FD‐like proteins required for their interactions, and demonstrate that 14‐3‐3 proteins are necessary bridges to mediate the FT1–TaFDL2 interaction. Using <italic>in vivo</italic> bimolecular fluorescent complementation (BiFC) assays, we demonstrate that the interaction between FT1 and 14‐3‐3 occurs in the cytoplasm, and that this complex is then translocated to the nucleus, where it interacts with TaFDL2 to form a FAC. We also demonstrate that a FAC including FT1, TaFDL2 and Ta14‐3‐3C can bind to the <italic>VRN1</italic> promoter <italic>in vitro</italic>. Finally, we show that relative transcript levels of<abstract abstract-type="main" id="tpj12960-abs-0001"> <title>Summary</title> <p>The FLOWERING LOCUS T (FT) protein is a central component of a mobile flowering signal (florigen) that is transported from leaves to the shoot apical meristem (SAM). Two FT monomers and two DNA‐binding bZIP transcription factors interact with a dimeric 14‐3‐3 protein bridge to form a hexameric protein complex. This complex, designated as the 'florigen activation complex' (FAC), plays a critical role in flowering. The wheat homologue of FT, designated FT1 (= VRN3), activates expression of <italic>VRN1</italic> in the leaves and the SAM, promoting flowering under inductive long days. In this study, we show that FT1, other FT‐like proteins, and different FD‐like proteins, can interact with multiple wheat and barley 14‐3‐3 proteins. We also identify the critical amino acid residues in FT1 and FD‐like proteins required for their interactions, and demonstrate that 14‐3‐3 proteins are necessary bridges to mediate the FT1–TaFDL2 interaction. Using <italic>in vivo</italic> bimolecular fluorescent complementation (BiFC) assays, we demonstrate that the interaction between FT1 and 14‐3‐3 occurs in the cytoplasm, and that this complex is then translocated to the nucleus, where it interacts with TaFDL2 to form a FAC. We also demonstrate that a FAC including FT1, TaFDL2 and Ta14‐3‐3C can bind to the <italic>VRN1</italic> promoter <italic>in vitro</italic>. Finally, we show that relative transcript levels of <italic>FD‐like</italic> and <italic>14‐3‐3</italic> genes vary among tissues and developmental stages. Since FD‐like proteins determine the DNA specificity of the FACs, variation in <italic>FD‐like</italic> gene expression can result in spatial and temporal modulation of the effects of mobile FT‐like signals.</p> </abstract> … (more)
- Is Part Of:
- Plant journal. Volume 84:Number 1(2015:Oct.)
- Journal:
- Plant journal
- Issue:
- Volume 84:Number 1(2015:Oct.)
- Issue Display:
- Volume 84, Issue 1 (2015)
- Year:
- 2015
- Volume:
- 84
- Issue:
- 1
- Issue Sort Value:
- 2015-0084-0001-0000
- Page Start:
- 70
- Page End:
- 82
- Publication Date:
- 2015-09-06
- Subjects:
- 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.12960 ↗
- 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:
- 3799.xml