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1H, 13C and 15N resonance assignments of a C-terminal domain of human CHD1

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Abstract

Chromatin remodelling proteins are an essential family of eukaryotic proteins. They harness the energy from ATP hydrolysis and apply it to alter chromatin structure in order to regulate all aspects of genome biology. Chromodomain helicase DNA-binding protein 1 (CHD1) is one such remodelling protein that has specialised nucleosome organising abilities and is conserved across eukaryotes. CHD1 possesses a pair of tandem chromodomains that directly precede the core catalytic Snf2 helicase-like domain, and a C-terminal SANT-SLIDE DNA-binding domain. We have identified an additional conserved domain in the C-terminal region of CHD1. Here, we report the backbone and side chain resonance assignments for this domain from human CHD1 at pH 6.5 and 25 °C (BMRB No. 25638).

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Acknowledgments

This work was supported by a Grant (1063301) from the National Health and Medical Research Council of Australia (NHMRC). J.P.M. was supported by an NHMRC Senior Research Fellowship (1058916). D.P.R. was supported by a NHMRC CJ Martin (Biomedical) Fellowship (457137).

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Authors and Affiliations

  1. School of Molecular Bioscience, The University of Sydney, Building G08, Corner Butlin Avenue and Maze Crescent, Sydney, NSW, 2006, Australia

    Biswaranjan Mohanty, Ana P. G. Silva & Joel P. Mackay

  2. Department of Genome Sciences, The John Curtin School of Medical Research, The Australian National University, Building 131, Garran Road, Canberra, ACT, 2601, Australia

    Daniel P. Ryan

  3. Faculty of Pharmacy and Pharmaceutical Sciences, Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, Melbourne, 3052, Australia

    Biswaranjan Mohanty

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  1. Biswaranjan Mohanty
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  2. Ana P. G. Silva
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  3. Joel P. Mackay
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Correspondence to Joel P. Mackay or Daniel P. Ryan.

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Mohanty, B., Silva, A.P.G., Mackay, J.P. et al. 1H, 13C and 15N resonance assignments of a C-terminal domain of human CHD1. Biomol NMR Assign 10, 31–34 (2016). https://doi.org/10.1007/s12104-015-9631-1

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  • DOI: https://doi.org/10.1007/s12104-015-9631-1

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