Judd Christopher Rice, PhD

Associate Professor of Cancer Biology

Director, Biochemistry & Molecular Medicine Master's Degree Program

Culture and Engagement Champion

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Overview

Each human chromosome contains 50-250 x 10e6 base pairs of DNA that compacts into an orderly structure by interacting with chromosomal proteins. Together, the DNA and these chromosomal proteins are generically described as chromatin. In eukaryotic organisms, the ability to precisely regulate nuclear processes is hindered by the inherently repressive chromatin environment where DNA is tightly packaged with chromosomal proteins. The fundamental structural unit of chromatin is the nucleosome which consists of the core histone octamer (two each of histone proteins H2A, H2B, H3 and H4) and the associated 146 base pairs of DNA that wraps twice around them. The N-terminal “tails” of the histones protrude from the nucleosome to interact with the nuclear environment. The enzymatic addition or removal of various post-translational modifications on histones generates a “histone code” at specific genomic regions that directly function to regulate specific DNA-templated processes including transcription, replication, repair, recombination and chromosome structure. Importantly, the activities of chromatin-modifying proteins are frequently altered in many human pathologies including developmental and age-related diseases, such as cancer.

The overall goal of my lab is to elucidate the factors that establish and maintain the “histone code” and how their concerted functions regulate essential chromatin-dependent events including transcription, DNA replication and DNA repair. This is accomplished using a combination of conventional biochemical approaches and state-of-the-art technologies. Our long term goal is to translate these fundamental biological insights into novel epigenetic therapies for the treatment of human diseases.

Research Funding

  • Advancing an Innovative NGS Approach to Discover and Investigate Histone Tail Proteolysis
    NIH · R21HG012833 · Feb 17, 2023 – Jan 31, 2025 · Role: Principal Investigator
  • Histone Proteolysis as a Novel Regulator of Myogenic Activation
    NIH · R21AR074649 · Dec 1, 2018 – Nov 30, 2021 · Role: Principal Investigator
  • Molecular mechanisms of gene silencing by H4 methylation
    NIH · R01GM075094 · Aug 1, 2007 – Jul 31, 2012 · Role: Principal Investigator
  • Epigenetic silencing by histone methylation
    NIH · F32GM064279 · Jun 25, 2001 – Oct 31, 2003 · Role: Principal Investigator

Publications

  • Leveraging Zymography to Discover and Investigate Nuclear Proteases. Methods Mol Biol. 2025; 2917:151-161.. View in PubMed
  • The MMP-2 histone H3 N-terminal tail protease is selectively targeted to the transcription start sites of active genes. Epigenetics Chromatin. 2023 05 10; 16(1):16.. View in PubMed
  • MMP-2 is a novel histone H3 N-terminal protease necessary for myogenic gene activation. Epigenetics Chromatin. 2021 05 17; 14(1):23.. View in PubMed
  • Effect of Periodized Resistance Training on Skeletal Muscle During Androgen Deprivation Therapy for Prostate Cancer: A Pilot Randomized Trial. Integr Cancer Ther. 2021 Jan-Dec; 20:15347354211035442.. View in PubMed
  • A pilot randomised controlled trial of a periodised resistance training and protein supplementation intervention in prostate cancer survivors on androgen deprivation therapy. BMJ Open. 2017 Jul 10; 7(7):e016910.. View in PubMed
  • The SUV4-20 inhibitor A-196 verifies a role for epigenetics in genomic integrity. Nat Chem Biol. 2017 03; 13(3):317-324.. View in PubMed
  • Acute Response of PGC-1α and IGF-1 Isoforms to Maximal Eccentric Exercise in Skeletal Muscle of Postmenopausal Women. J Strength Cond Res. 2016 Apr; 30(4):1161-70.. View in PubMed
  • MMP-9 facilitates selective proteolysis of the histone H3 tail at genes necessary for proficient osteoclastogenesis. Genes Dev. 2016 Jan 15; 30(2):208-19.. View in PubMed
  • Cooperation between SMYD3 and PC4 drives a distinct transcriptional program in cancer cells. Nucleic Acids Res. 2015 Oct 15; 43(18):8868-83.. View in PubMed
  • Small-molecule inhibitors of SETD8 with cellular activity. ACS Chem Biol. 2014 Nov 21; 9(11):2471-8.. View in PubMed