Dr Chris Millard

Our goal is to understand how gene expression is regulated through the recruitment of proteins to chromatin. We study one particular family of proteins called histone deacetylases which dictate higher-order chromatin structure through the modification of histone tails. The removal of a single acetyl mark from these unstructured histone tails has the potential to influence many fundamental biological processes.

I have been part of the Schwabe group at the University of Leicester since 2010 where we work to understand the structure and function of Histone Deacetylase complexes. Previous to my current post, I completed my PhD in Structural Biology at the University of Oxford in 2008, and held a post-doc position at Monash University, Australia. Between 2020-24 I took a five-year career break from academia to look after family, held part-time roles at UKHSA (public health), elected as a school governor and became a qualified orienteering coach.

We are currently using cryo-electron microscopy to study six different histone-containing complexes as well as developing an understanding of their function within the cell.

ORCID: https://orcid.org/0000-0002-1012-0829

Research highlights

Millard CJ, Fairall L, Ragan, TJ, Savva CG, Schwabe JWR. (2020) The topology of chromatin-binding domains in the NuRD deacetylase complex. Nucleic Acids Res. 48:12972-12982.

Watson PJ*, Millard CJ*, Riley AM, Robertson NS, Wright, LC, Godage HY, Cowley SM, Jamieson AG, Potter BVL, Schwabe JWR. (2016) Insights into the activation mechanism of class I HDAC complexes by inositol phosphates. Nat Commun. 7:11262.

Millard CJ, Varma N, Saleh A, Morris K, Watson PJ, Bottrill AR, Fairall L, Smith CJ, Schwabe JWR. (2016) The structure of the core NuRD complex provides insights into its interaction with chromatin. eLife 5:e13941.

Millard CJ, Ludeman JP, Canals M, Bridgford JL, Hinds MG, Clayton DJ, Christopoulos A, Payne RJ, Stone MJ. (2014) Structural basis of receptor sulfotyrosine recognition by a CC chemokine: the N-terminal region of CCR3 bound to CCL11/eotaxin-1. Structure 22:1571-81.

Millard CJ, Watson PJ, Celardo I, Gordiyenko Y, Cowley SM, Robinson CV, Fairall L, and Schwabe JWR. (2013) Class I HDACs share a common mechanism of regulation by inositol phosphates. Mol Cell. 51:57-67.

Other recent publications

Archibald LJ, Brown EA, Millard CJ, Watson PJ, Robertson, N, Wang, S, Schwabe, JWR. Jamieson, A. (2022) Hydroxamic acid-modified peptide library provides insights into the molecular basis for the substrate selectivity of HDAC corepressor complexes. ACS Chem Biol. 17(9):2572-2582.

Turnbull, R, Fairall, L, Saleh, A, Kesall, E, Morris, K, Ragan, T, Savva, C, Chandru, A, Millard, CJ, Makarvova, O, Smith, C, Rosemann, A, Fry, A, Cowley, SM, Schwabe, JWR. (2020) The MiDAC histone deacetylase complex is essential for embryonic development and has a unique multivalent structure. Nature Communications 11, 3252.

Millard, CJ, Fairall, L, Ragan, TJ, Savva, CG, and Schwabe, JWR. (2020) The topology of chromatin-binding domains in the NuRD deacetylase complex. Nucleic Acids Research 48, 12972.

Wang, ZA, Millard, CJ, Lin, C-L, Gurnett, J, Wu, M, Lee, K, Fairall, L, Schwabe, JWR, Cole, PA. (2020) Diverse Nucleosome Site-Selectivity Among Histone Deacetylase Complexes. eLife 9, e57663. 

Smalley, J, Adams, G, Millard, CJ, Song, Y, Schwabe, JWR, Cowley, SM, Hodgkinson, JT. (2020) PROTAC mediated degradation of Class-I histone deacetylase enzymes in corepressor complexes. Chemical Communications doi: 10.1039/d0cc01485k.