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Molecular determinants of complex formation between DNA and the AT ‐rich interaction domain of BAF 250a
Author(s) -
Maulik Aditi,
Giri Malyasree,
Singh Mahavir
Publication year - 2019
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13540
Subject(s) - dna , arid , chemistry , binding site , biophysics , biochemistry , chromatin , dna binding protein , plasma protein binding , dna supercoil , hmg box , computational biology , biology , genetics , microbiology and biotechnology , transcription factor , ecology , dna replication , gene
AT ‐rich interaction domain ( ARID )‐containing BAF 250a protein is a central DNA ‐binding subunit of the SWI / SNF chromatin‐remodeling complex. ARID s are found in several eukaryotic proteins that play roles in different aspects of cellular physiology. However, despite their biological importance, ARID s remain relatively uncharacterized for their dynamics and DNA binding. Here, we have probed the structure and DNA ‐binding properties of BAF 250a ARID . We show that the core BAF 250a ARID interacts with DNA sequences with low micromolar affinities. NMR chemical shift perturbation ( CSP ) results reveal a number of conserved residues in ARID that are involved in DNA binding. An NMR CSP ‐based docking model of ARID – DNA complexes reveals that BAF 250a ARID possesses necessary determinants of specific DNA binding.