The genomic DNA of higher organisms winds around hockey-puck like octamers, comprised of histone proteins, forming chromatin fibers that further coil into chromosomes.
The genomic DNA of higher organisms winds around hockey-puck like octamers, comprised of histone proteins, forming chromatin fibers that further coil into chromosomes. Histone proteins and many of their regulators and chaperones play a critical role in shepherding the gene accessibility within cells in various tissues, but also when genetic information is passed from one generation to another. Misregulation of chromatin is implicated in numerous human genetic diseases, including brain disorders and cancer. Garegin Papoian, Yamini Dalal, and colleagues have combined molecular dynamics simulations and in vivo experiments to gain new insights on the interactions between a key histone chaperone protein, Holliday Junction Recognition Protein (HJURP), and the histones CENP-A and H4, where the latter are responsible for the packaging of centromeric DNA in human chromosomes, which is essential for mitosis (DOI: 10.1021/jacs.6b05355).
Their findings show how these HJURP chaperones facilitate folding, prevent mis-binding and help guide correct interactions between histones themselves and also other centromeric proteins, uncovering how HJURP nudges along the assembly processes of CENP-A nucleosomes and the corresponding higher-order centromeric structures. This research is featured on the cover of the Oct. 12 issue of the Journal of the American Chemical Society (JACS), and as a JACS spotlight (put link here).
Prof. Garyk Papoian is the Monroe Martin Professor in the Dept. of Chemistry & Biochemistry and I.P.S.T. at the University of Maryland, where he directs a multidisciplinary research group on theoretical biophysical chemistry. His group develops and utilizes advanced computational methods to probe biological processes on lengthscales that range from the molecular to cellular regimes.
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