Specific interactions between the K domains of AG and AGLs, members of the MADS domain family of DNA binding proteins

Fan, H. Y., Hu, Y., Tudor, M., Ma, H. (November 1997) Specific interactions between the K domains of AG and AGLs, members of the MADS domain family of DNA binding proteins. Plant Journal, 12 (5). pp. 999-1010. ISSN 0960-7412

URL: http://www.ncbi.nlm.nih.gov/pubmed/9418042
DOI: 10.1046/j.1365-313X.1997.12050999.x

Abstract

MADS domain (for MCM1, AG, DEFA and SRF) proteins are regulatory proteins found in all major eukaryotic kingdoms. Plant MADS domain regulatory proteins have a region of moderate sequence similarity that has been designated as the K domain, and its predicted coiled-coil structure suggests a role in establishing a protein-protein interaction. In vivo studies with the Arabidopsis AGAMOUS (AG) protein have indicated that the K domain is important for AG function. Using a bait fusion protein containing the K domain and the C-terminal region of AG in a yeast two-hybrid selection, 156 clones that encode potential AG-interacting proteins were identified. These clones each encode one of four highly related MADS domain proteins: AGL2, AGL4, AGL6 and AGL9. Additional analysis showed that the K domain of AG alone was able to bind the K domains of these AGLs. This binding was further confirmed by immunoprecipitation experiments using in vitro synthesized AG and AGL K domains. These results strongly suggest that AG interacts with AGL2, AGL4, AGL6 and AGL9 in vivo. Based on these results and previous observations, it is proposed that the AG function requires interaction with at least one of these AGL proteins, and such interactions contribute to the functional specificity of the AG protein.

Item Type: Paper
Uncontrolled Keywords: AGAMOUS Protein, Arabidopsis Amino Acid Sequence Arabidopsis/ metabolism Base Sequence Binding Sites Cloning, Molecular DNA, Plant/metabolism DNA-Binding Proteins/ chemistry/ metabolism Molecular Sequence Data Plant Proteins/ chemistry/ metabolism Protein Conformation Recombinant Fusion Proteins/chemistry/metabolism Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Restriction Mapping Saccharomyces cerevisiae Sequence Homology, Amino Acid beta-Galactosidase/metabolism
Subjects: organism description > plant > Arabidopsis
organism description > yeast > Saccharomyces
Investigative techniques and equipment > cloning
Investigative techniques and equipment > assays > cloning

bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
CSHL Authors:
Communities: CSHL labs
Depositing User: Kathleen Darby
Date: November 1997
Date Deposited: 07 May 2014 15:14
Last Modified: 07 May 2014 15:14
Related URLs:
URI: http://repository.cshl.edu/id/eprint/30027

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