Mayo researchers provide atomic view of a histone chaperone

Posted on March 2nd, 2012 by

Mayo Clinic researchers have gained insights into the function of a member of a family of specialized proteins called histone chaperones. Using nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography, they have determined the 3-D structure and interactions of the histone chaperone Rtt106 down to the atomic details. The findings are published in the journal Nature. "The interactions we described are important for gene silencing and the DNA damage response," says senior author Georges Mer, Ph.D., a Mayo Clinic structural biologist. "This is exciting because our newfound knowledge will help us better understand these fundamental cellular processes."

Science Codex, 03/01/2012

Tags: Georges Mer, histone chaperones, Nature, NMR, nuclear magnetic resonance spectroscopy, Research, Rtt106, specialized proteins, structural biologist, X-ray crystallography

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