Chunyuan Jin

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Chunyuan Jin

Assistant Professor, Department of Environmental Medicine
Assistant Professor, Department of Biochemistry and Molecular Pharmacology


Contact Info

Address
57 Old Forge Rd.
Tuxedo, NY 10987

845-731-3602
Chunyuan.Jin@nyumc.org

Research Summary

In eukaryotic cells, DNA is packaged into a DNA-protein complex called chromatin. The fundamental subunit of chromatin is the nucleosome core particle, which consists of 147 base pairs of DNA wrapped around a histone octamer. Chromatin structure regulates the access of regulatory factors to the genomic DNA and thus exerts a profound control over most DNA-templated processes such as transcription, DNA repair and replication. Elucidating the interaction between chromatin structure and these nuclear processes is critical for understanding of development and human disease. Chromatin structure can be altered by several epigenetic mechanisms including DNA methylation, post-translational histone modifications, and the assembly of variant histones into chromatin. Our research focuses on how epigenetic mechanisms, in particular the incorporation of histone variants into nucleosome, modulate chromatin structure and gene expression. Another focus in our laboratory involves understanding the mechanisms of both assembly/disassembly and replication of nucleosomes containing histone variant(s). We are also interested in the mechanisms by which environmental factors influence epigenetic profiles of normal cells and contribute to carcinogenesis.

Research Keywords

chromatin structure, epigenetic mechanisms, histone variants, gene expression, carcinogenesis, cancer, genome integrity

Mechanisms Underlying Acrolein-mediated Inhibition of Chromatin Assembly
Fang, Lei; Chen, Danqi; Yu, Clinton; Li, Hongjie; Brocato, Jason; Huang, Lan; Jin, Chunyuan. Mechanisms Underlying Acrolein-mediated Inhibition of Chromatin Assembly. Molecular & cellular biology. 2016 Dec 01;36(23):2995-3008 (2262242)

Hexavalent Chromium (Cr(VI)) Down-Regulates Acetylation of Histone H4 at Lysine 16 through Induction of Stressor Protein Nupr1
Chen, Danqi; Kluz, Thomas; Fang, Lei; Zhang, Xiaoru; Sun, Hong; Jin, Chunyuan; Costa, Max. Hexavalent Chromium (Cr(VI)) Down-Regulates Acetylation of Histone H4 at Lysine 16 through Induction of Stressor Protein Nupr1. PLoS one. 2016 ;11(6):e0157317-e0157317 e0157317 (2136612)

A Potential New Mechanism of Arsenic Carcinogenesis: Depletion of Stem-Loop Binding Protein and Increase in Polyadenylated Canonical Histone H3.1 mRNA
Brocato, Jason; Chen, Danqi; Liu, Jianli; Fang, Lei; Jin, Chunyuan; Costa, Max. A Potential New Mechanism of Arsenic Carcinogenesis: Depletion of Stem-Loop Binding Protein and Increase in Polyadenylated Canonical Histone H3.1 mRNA. Biological trace element research. 2015 Jul;166(1):72-81 (1587302)

Arsenic induces polyadenylation of canonical histone mRNA by downregulating stem-loop binding protein gene expression
Brocato, Jason; Fang, Lei; Chervona, Yana; Chen, Danqi; Kiok, Kathrin; Sun, Hong; Tseng, Hsiang-Chi; Xu, Dazhong; Shamy, Magdy; Jin, Chunyuan; Costa, Max. Arsenic induces polyadenylation of canonical histone mRNA by downregulating stem-loop binding protein gene expression. Journal of biological chemistry. 2014 Nov 14;289(46):31751-31764 (1282832)

Arsenic epigenetically regulates SLBP which leads to aberrant polyadenylation of h3.1 mRNA that remains present outside of s phase
Brocato, J A; Chervona, Y; Jin, C; Costa, M. Arsenic epigenetically regulates SLBP which leads to aberrant polyadenylation of h3.1 mRNA that remains present outside of s phase [Meeting Abstract]. Environmental & molecular mutagenesis. 2014 Sep;55:S60-S60 (1291782)