Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 445225
Title Structural determinants of DNA recognition by plant MADS-domain transcription factors
Author(s) Muino Acuna, J.M.; Smaczniak, C.; Angenent, G.C.; Kaufmann, K.; Dijk, A.D.J. van
Source Nucleic Acids Research 42 (2014)4. - ISSN 0305-1048 - p. 2138 - 2146.
Department(s) PRI BIOS Applied Bioinformatics
Laboratory of Molecular Biology
PRI BIOS Plant Development Systems
Biometris (WU MAT)
Publication type Refereed Article in a scientific journal
Publication year 2014
Keyword(s) in-vitro - binding properties - flower development - antirrhinum-majus - homeotic proteins - crystal-structure - ternary complex - floral organs - box proteins - chip-chip
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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