A subcellular tug of war involving three MYB‐like proteins underlies a molecular antagonism in Antirrhinum flower asymmetry. (30th May 2013)
- Record Type:
- Journal Article
- Title:
- A subcellular tug of war involving three MYB‐like proteins underlies a molecular antagonism in Antirrhinum flower asymmetry. (30th May 2013)
- Main Title:
- A subcellular tug of war involving three MYB‐like proteins underlies a molecular antagonism in Antirrhinum flower asymmetry
- Authors:
- Raimundo, João
Sobral, Rómulo
Bailey, Paul
Azevedo, Herlânder
Galego, Lisete
Almeida, Jorge
Coen, Enrico
Costa, Maria Manuela R. - Abstract:
- <abstract abstract-type="main" id="tpj12225-abs-0001"> <title>Summary</title> <p>The establishment of meristematic domains with different transcriptional activity is essential for many developmental processes. The asymmetry of the <italic>Antirrhinum majus</italic> flower is established by transcription factors with an asymmetric pattern of activity. To understand how this asymmetrical pattern is established, we studied the molecular mechanism through which the dorsal MYB protein RADIALIS (RAD) restricts the activity of the MYB transcription factor DIVARICATA (DIV) to the ventral region of the flower meristem. We show that RAD competes with DIV for binding with other MYB‐like proteins, termed DRIF1 and DRIF2 (DIV‐ and‐RAD‐interacting‐factors). DRIF1 and DIV interact to form a protein complex that binds to the DIV‐DNA consensus region, suggesting that the DRIFs act as co‐regulators of DIV transcriptional activity. In the presence of RAD, the interaction between DRIF1 and DIV bound to DNA is disrupted. Moreover, the DRIFs are sequestered in the cytoplasm by RAD, thus, preventing or reducing the formation of DRIF‐DIV heterodimers in the nuclei. Our results suggest that in the dorsal region of the <italic>Antirrhinum</italic> flower meristem the dorsal protein RAD antagonises the activity of the ventral identity protein DIV in a subcellular competition for a DRIF protein promoting the establishment of the asymmetric pattern of gene activity in the <italic>Antirrhinum</italic><abstract abstract-type="main" id="tpj12225-abs-0001"> <title>Summary</title> <p>The establishment of meristematic domains with different transcriptional activity is essential for many developmental processes. The asymmetry of the <italic>Antirrhinum majus</italic> flower is established by transcription factors with an asymmetric pattern of activity. To understand how this asymmetrical pattern is established, we studied the molecular mechanism through which the dorsal MYB protein RADIALIS (RAD) restricts the activity of the MYB transcription factor DIVARICATA (DIV) to the ventral region of the flower meristem. We show that RAD competes with DIV for binding with other MYB‐like proteins, termed DRIF1 and DRIF2 (DIV‐ and‐RAD‐interacting‐factors). DRIF1 and DIV interact to form a protein complex that binds to the DIV‐DNA consensus region, suggesting that the DRIFs act as co‐regulators of DIV transcriptional activity. In the presence of RAD, the interaction between DRIF1 and DIV bound to DNA is disrupted. Moreover, the DRIFs are sequestered in the cytoplasm by RAD, thus, preventing or reducing the formation of DRIF‐DIV heterodimers in the nuclei. Our results suggest that in the dorsal region of the <italic>Antirrhinum</italic> flower meristem the dorsal protein RAD antagonises the activity of the ventral identity protein DIV in a subcellular competition for a DRIF protein promoting the establishment of the asymmetric pattern of gene activity in the <italic>Antirrhinum</italic> flower.</p> </abstract> … (more)
- Is Part Of:
- Plant journal. Volume 75:Number 4(2013:Aug.)
- Journal:
- Plant journal
- Issue:
- Volume 75:Number 4(2013:Aug.)
- Issue Display:
- Volume 75, Issue 4 (2013)
- Year:
- 2013
- Volume:
- 75
- Issue:
- 4
- Issue Sort Value:
- 2013-0075-0004-0000
- Page Start:
- 527
- Page End:
- 538
- Publication Date:
- 2013-05-30
- 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.12225 ↗
- 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:
- 3892.xml