DNA-binding properties of the recombinant high-mobility-group-like AT-hook-containing region from human BRG1 protein
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Mahavir Singh
Abstract
The hBRG1 protein, a central ATPase of the human switching/sucrose non-fermenting (SWI/SNF) remodeling complex, has a catalytic ATPase domain, an AT-hook motif and a bromodomain. Bromodomains, found in many chromatin-associated proteins, recognize N-acetyl-lysine in histones and other proteins. The AT-hook motif, first described in the high-mobility group of non-histone chromosomal proteins HMGA1/2, is a DNA-binding motif. The AT-hook binds to the AT-rich DNA sequences in the minor groove of B-DNA in a non-sequence specific manner. AT-hook motifs have been identified in many other DNA-binding proteins. In this study we cloned and purified a fragment of hBRG1 encompassing the AT-hook region and the bromodomain. Nuclear magnetic resonance (NMR) and circular dichroism (CD) analyses show that the recombinant domains are structured. The functionality of subdomains was checked by assessing their interactions with N-acetylated peptides from histones and with DNA. Isothermal titration calorimetric (ITC) analysis demonstrates that the primary micromolar interaction is through the AT-hook motif. The AT-hook region binds to linear DNA by unwinding it. These properties resemble the characteristics of the HMGA1/2 proteins and their interaction with DNA.
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Articles in the same Issue
- Highlight: Redox signaling – mechanisms and biological impact
- Paper of the Year 2005: Award to Vanessa Ferreira Merino
- Two-site substrate recognition model for the Keap1-Nrf2 system: a hinge and latch mechanism
- Hypoxia and lipid signaling
- Glutathione peroxidases and redox-regulated transcription factors
- Redox regulation of the hypoxia-inducible factor
- The l-arginine nitric oxide pathway: avenue for a multiple-level approach to assess vascular function
- Protein oxidation and proteolysis
- Mitochondrial signaling, TOR, and life span
- Pathogenetic interplay between osmotic and oxidative stress: the hepatic encephalopathy paradigm
- Regulation of redox-sensitive exofacial protein thiols in CHO cells
- N-Ethylmaleimide-sensitive factor: a redox sensor in exocytosis
- Aspects of the biological redox chemistry of cysteine: from simple redox responses to sophisticated signalling pathways
- Singlet oxygen inactivates protein tyrosine phosphatase-1B by oxidation of the active site cysteine
- Regulatory effects of the mitochondrial energetic status on mitochondrial p66Shc
- Air pollution-associated fly ash particles induce fibrotic mechanisms in primary fibroblasts
- Incinerator fly ash provokes alteration of redox equilibrium and liberation of arachidonic acid in vitro
- Unique neuronal functions of cathepsin L and cathepsin B in secretory vesicles: biosynthesis of peptides in neurotransmission and neurodegenerative disease
- Two novel mitochondrial and chloroplastic targeting-peptide-degrading peptidasomes in A. thaliana, AtPreP1 and AtPreP2
- Switch from actin α1 to α2 expression and upregulation of biomarkers for pressure overload and cardiac hypertrophy in taurine-deficient mouse heart
- Human RBM28 protein is a specific nucleolar component of the spliceosomal snRNPs
- The β12-β13 loop is a key regulatory element for the activity and properties of the catalytic domain of protein phosphatase 1 and 2B
- DNA-binding properties of the recombinant high-mobility-group-like AT-hook-containing region from human BRG1 protein
- Papaya glutamine cyclotransferase shows a singular five-fold β-propeller architecture that suggests a novel reaction mechanism
- First identification of a phosphorylcholine-substituted protein from Caenorhabditis elegans: isolation and characterization of the aspartyl protease ASP-6
- The human cathelicidin peptide LL-37 and truncated variants induce segregation of lipids and proteins in the plasma membrane of Candida albicans
- Specificity of human cathepsin S determined by processing of peptide substrates and MHC class II-associated invariant chain
- Mast cell-dependent activation of pro matrix metalloprotease 2: a role for serglycin proteoglycan-dependent mast cell proteases