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

  • Dynamic regulation of the PR-Set7 histone methyltransferase is required for normal cell cycle progression. Genes Dev. 2010 Nov 15; 24(22):2531-42.. View in PubMed
  • Role for the nuclear receptor-binding SET domain protein 1 (NSD1) methyltransferase in coordinating lysine 36 methylation at histone 3 with RNA polymerase II function. Proc Natl Acad Sci U S A. 2010 Sep 28; 107(39):16952-7.. View in PubMed
  • PR-Set7-mediated monomethylation of histone H4 lysine 20 at specific genomic regions induces transcriptional repression. J Cell Biochem. 2010 Jun 01; 110(3):609-19.. View in PubMed
  • A histone methylation code for SV40 minichromosomes. Cell Cycle. 2010 Apr 01; 9(7):1235-6.. View in PubMed
  • Hormone replacement therapy and messenger RNA expression of estrogen receptor coregulators after exercise in postmenopausal women. Med Sci Sports Exerc. 2010 Mar; 42(3):422-9.. View in PubMed
  • Exercise does not influence myostatin and follistatin messenger RNA expression in young women. J Strength Cond Res. 2010 Feb; 24(2):522-30.. View in PubMed
  • Influence of hormone replacement therapy on eccentric exercise induced myogenic gene expression in postmenopausal women. J Appl Physiol (1985). 2009 Nov; 107(5):1381-8.. View in PubMed
  • Identification and characterization of posttranslational modification-specific binding proteins in vivo by mammalian tethered catalysis. Proc Natl Acad Sci U S A. 2009 Sep 01; 106(35):14808-13.. View in PubMed
  • Hormone therapy attenuates exercise-induced skeletal muscle damage in postmenopausal women. J Appl Physiol (1985). 2009 Sep; 107(3):853-8.. View in PubMed
  • Catalytic function of the PR-Set7 histone H4 lysine 20 monomethyltransferase is essential for mitotic entry and genomic stability. J Biol Chem. 2008 Jul 11; 283(28):19478-88.. View in PubMed