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Biochemistry: Unspooling DNA from nucleosomal disks
Date:5/23/2013

ndele, first author of the new study. "However, using high-resolution X-ray crystallography, we were ultimately able to determine the structure of the whole complex formed between FACT and the histone dimer."

The conformation of the complex revealed that binding of FACT blocks a site on the histone dimer that has a high affinity for DNA. This interaction releases the DNA from the nucleosome sufficiently to permit gene transcription to proceed past the nucleosome. "And in contrast to the conventional view, this mechanism works without unwrapping the DNA completely from the nucleosome," says Ladurner. Thus, the new study affords detailed insights into the mechanisms underlying the dynamic regulation of chromatin accessibility in the cell nucleus.


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Contact: Luise Dirscherl
dirscherl@lmu.de
49-892-180-2706
Ludwig-Maximilians-Universitt Mnchen
Source:Eurekalert

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