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  Structural determinants of DNA recognition by plant MADS-domain transcription factors

Muino, J. M., Smaczniak, C., Angenent, G. C., Kaufmann, K., & van Dijk, A. D. (2014). Structural determinants of DNA recognition by plant MADS-domain transcription factors. Nucleic Acids Research (London), 42(4), 2138-2146. doi:10.1093/nar/gkt1172.

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© 2014 Oxford University Press
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Muino, J. M.1, Author              
Smaczniak, C., Author
Angenent, G. C., Author
Kaufmann, K., Author
van Dijk, A. D., Author
Affiliations:
1Dept. of Computational Molecular Biology (Head: Martin Vingron), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433547              

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Free keywords: Arabidopsis Proteins/metabolism Base Sequence Binding Sites Consensus Sequence DNA, Plant/*chemistry/metabolism Homeodomain Proteins/metabolism MADS Domain Proteins/*metabolism Nucleic Acid Conformation Nucleotide Motifs Plant Proteins/*metabolism Protein Binding Transcription Factors/metabolism
 Abstract: Plant MADS-domain transcription factors act as key regulators of many developmental processes. Despite the wealth of information that exists about these factors, the mechanisms by which they recognize their cognate DNA-binding site, called CArG-box (consensus CCW6GG), and how different MADS-domain proteins achieve DNA-binding specificity, are still largely unknown. We used information from in vivo ChIP-seq experiments, in vitro DNA-binding data and evolutionary conservation to address these important questions. We found that structural characteristics of the DNA play an important role in the DNA binding of plant MADS-domain proteins. The central region of the CArG-box largely resembles a structural motif called 'A-tract', which is characterized by a narrow minor groove and may assist bending of the DNA by MADS-domain proteins. Periodically spaced A-tracts outside the CArG-box suggest additional roles for this structure in the process of DNA binding of these transcription factors. Structural characteristics of the CArG-box not only play an important role in DNA-binding site recognition of MADS-domain proteins, but also partly explain differences in DNA-binding specificity of different members of this transcription factor family and their heteromeric complexes.

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Language(s): eng - English
 Dates: 2013-11-252014-02
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1093/nar/gkt1172
ISSN: 1362-4962 (Electronic)0305-1048 (Print)
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Title: Nucleic Acids Research (London)
  Other : Nucleic Acids Res
Source Genre: Journal
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Publ. Info: Oxford : Oxford University Press
Pages: - Volume / Issue: 42 (4) Sequence Number: - Start / End Page: 2138 - 2146 Identifier: ISSN: 0305-1048
CoNE: https://pure.mpg.de/cone/journals/resource/110992357379342