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PMID: 9243505 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Determination of floral organ identity by Arabidopsis MADS domain homeotic proteins AP1, AP3, PI, and AG is independent of their DNA-binding specificity.

Molecular biology of the cell ·Vol. 8 ·No. 7 ·1997-07-00 ·Pages 1243-59

Riechmann JL, Meyerowitz EM

Abstract

The MADS domain homeotic proteins APETALA1 (AP1), APETALA3 (AP3), PISTILLATA (PI), and AGAMOUS (AG) combinatorially specify the identity of Arabidopsis floral organs. AP1/AP1, AG/AG, and AP3/PI dimers bind to similar CArG box sequences; thus, differences in DNA-binding specificity among these proteins do not seem to be the origin of their distinct organ identity properties. To assess the overall contribution that specific DNA binding could make to their biological specificity, we have generated chimeric genes in which the amino-terminal half of the MADS domain of AP1, AP3, PI, and AG was substituted by the corresponding sequences of human SRF and MEF2A proteins. In vitro DNA-binding assays reveal that the chimeric proteins acquired the respective, and distinct, DNA-binding specificity of SRF or MEF2A. However, ectopic expression of the chimeric genes reproduces the dominant gain-of-function phenotypes exhibited by plants ectopically expressing the corresponding Arabidopsis wild-type genes. In addition, both the SRF and MEF2 chimeric genes can complement the pertinent ap1-1, ap3-3, pi-1, or ag-3 mutations to a degree similar to that of AP1, AP3, PI, and AG when expressed under the control of the same promoter. These results indicate that determination of floral organ identity by the MADS domain homeotic proteins AP1, AP3, PI, and AG is independent of their DNA-binding specificity. In addition, the DNA-binding experiments show that either one of the two MADS domains of a dimer can be sufficient to confer a particular DNA-binding specificity to the complex and that sequences outside the amino-terminal basic region of the MADS domain can, in some cases, contribute to the DNA-binding specificity of the proteins.

MeSH Terms
AGAMOUS Protein, Arabidopsis Amino Acid Sequence Arabidopsis/anatomy & histology,genetics,metabolism Arabidopsis Proteins DNA-Binding Proteins/genetics,metabolism Homeodomain Proteins/genetics,metabolism MADS Domain Proteins Molecular Sequence Data Nuclear Proteins/genetics,metabolism Phenotype Plant Proteins/genetics,metabolism Recombinant Fusion Proteins/genetics,metabolism Transcription Factors/genetics,metabolism
Chemicals
AGAMOUS Protein, Arabidopsis AP1 protein, Arabidopsis APETALA 3 protein, Arabidopsis APETALA2 protein, Arabidopsis Arabidopsis Proteins DNA-Binding Proteins Homeodomain Proteins MADS Domain Proteins Nuclear Proteins PISTILLATA protein, Arabidopsis Plant Proteins Recombinant Fusion Proteins Transcription Factors
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Riechmann J L
Division of Biology, California Institute of Technology, Pasadena 91125, USA.
Meyerowitz E M
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Article Info
Journal
Molecular biology of the cell
Abbr.
Mol Biol Cell
ISSN
1059-1524
Published
1997-07-00
Pages
1243-59
Language
English
Region
United States
NLM ID
9201390
PMCID
PMC276150
Subset
IM
Grants
NIGMS NIH HHS · GM-45697 · United States
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