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SEPALLATA3: the 'glue' for MADS box transcription factor complex formation

BACKGROUND: Plant MADS box proteins play important roles in a plethora of developmental processes. In order to regulate specific sets of target genes, MADS box proteins dimerize and are thought to assemble into multimeric complexes. In this study a large-scale yeast three-hybrid screen is utilized t...

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Autores principales: Immink, Richard GH, Tonaco, Isabella AN, de Folter, Stefan, Shchennikova, Anna, van Dijk, Aalt DJ, Busscher-Lange, Jacqueline, Borst, Jan W, Angenent, Gerco C
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2688274/
https://www.ncbi.nlm.nih.gov/pubmed/19243611
http://dx.doi.org/10.1186/gb-2009-10-2-r24
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author Immink, Richard GH
Tonaco, Isabella AN
de Folter, Stefan
Shchennikova, Anna
van Dijk, Aalt DJ
Busscher-Lange, Jacqueline
Borst, Jan W
Angenent, Gerco C
author_facet Immink, Richard GH
Tonaco, Isabella AN
de Folter, Stefan
Shchennikova, Anna
van Dijk, Aalt DJ
Busscher-Lange, Jacqueline
Borst, Jan W
Angenent, Gerco C
author_sort Immink, Richard GH
collection PubMed
description BACKGROUND: Plant MADS box proteins play important roles in a plethora of developmental processes. In order to regulate specific sets of target genes, MADS box proteins dimerize and are thought to assemble into multimeric complexes. In this study a large-scale yeast three-hybrid screen is utilized to provide insight into the higher-order complex formation capacity of the Arabidopsis MADS box family. SEPALLATA3 (SEP3) has been shown to mediate complex formation and, therefore, special attention is paid to this factor in this study. RESULTS: In total, 106 multimeric complexes were identified; in more than half of these at least one SEP protein was present. Besides the known complexes involved in determining floral organ identity, various complexes consisting of combinations of proteins known to play a role in floral organ identity specification, and flowering time determination were discovered. The capacity to form this latter type of complex suggests that homeotic factors play essential roles in down-regulation of the MADS box genes involved in floral timing in the flower via negative auto-regulatory loops. Furthermore, various novel complexes were identified that may be important for the direct regulation of the floral transition process. A subsequent detailed analysis of the APETALA3, PISTILLATA, and SEP3 proteins in living plant cells suggests the formation of a multimeric complex in vivo. CONCLUSIONS: Overall, these results provide strong indications that higher-order complex formation is a general and essential molecular mechanism for plant MADS box protein functioning and attribute a pivotal role to the SEP3 'glue' protein in mediating multimerization.
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spelling pubmed-26882742009-05-29 SEPALLATA3: the 'glue' for MADS box transcription factor complex formation Immink, Richard GH Tonaco, Isabella AN de Folter, Stefan Shchennikova, Anna van Dijk, Aalt DJ Busscher-Lange, Jacqueline Borst, Jan W Angenent, Gerco C Genome Biol Research BACKGROUND: Plant MADS box proteins play important roles in a plethora of developmental processes. In order to regulate specific sets of target genes, MADS box proteins dimerize and are thought to assemble into multimeric complexes. In this study a large-scale yeast three-hybrid screen is utilized to provide insight into the higher-order complex formation capacity of the Arabidopsis MADS box family. SEPALLATA3 (SEP3) has been shown to mediate complex formation and, therefore, special attention is paid to this factor in this study. RESULTS: In total, 106 multimeric complexes were identified; in more than half of these at least one SEP protein was present. Besides the known complexes involved in determining floral organ identity, various complexes consisting of combinations of proteins known to play a role in floral organ identity specification, and flowering time determination were discovered. The capacity to form this latter type of complex suggests that homeotic factors play essential roles in down-regulation of the MADS box genes involved in floral timing in the flower via negative auto-regulatory loops. Furthermore, various novel complexes were identified that may be important for the direct regulation of the floral transition process. A subsequent detailed analysis of the APETALA3, PISTILLATA, and SEP3 proteins in living plant cells suggests the formation of a multimeric complex in vivo. CONCLUSIONS: Overall, these results provide strong indications that higher-order complex formation is a general and essential molecular mechanism for plant MADS box protein functioning and attribute a pivotal role to the SEP3 'glue' protein in mediating multimerization. BioMed Central 2009 2009-02-25 /pmc/articles/PMC2688274/ /pubmed/19243611 http://dx.doi.org/10.1186/gb-2009-10-2-r24 Text en Copyright © 2009 Immink et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an open access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research
Immink, Richard GH
Tonaco, Isabella AN
de Folter, Stefan
Shchennikova, Anna
van Dijk, Aalt DJ
Busscher-Lange, Jacqueline
Borst, Jan W
Angenent, Gerco C
SEPALLATA3: the 'glue' for MADS box transcription factor complex formation
title SEPALLATA3: the 'glue' for MADS box transcription factor complex formation
title_full SEPALLATA3: the 'glue' for MADS box transcription factor complex formation
title_fullStr SEPALLATA3: the 'glue' for MADS box transcription factor complex formation
title_full_unstemmed SEPALLATA3: the 'glue' for MADS box transcription factor complex formation
title_short SEPALLATA3: the 'glue' for MADS box transcription factor complex formation
title_sort sepallata3: the 'glue' for mads box transcription factor complex formation
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2688274/
https://www.ncbi.nlm.nih.gov/pubmed/19243611
http://dx.doi.org/10.1186/gb-2009-10-2-r24
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