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CSHL researchers explain process by which cells 'hide' potentially dangerous DNA segments
Date:4/9/2009

tromeres are crucial for genomic integrity, aberrant heterochromatin formation can result in genetic anomalies and diseases such as cancer.

Heterochromatin depends on the density of chemical "marks" that are added to histones at specific locations on their tail ends. These marks consist of methyl groups that get attached to the tail of one of the histones, histone H3, at a specific spot the ninth residue, which happens to be the amino acid lysine (K). This mark is therefore called H3K9me.

In fission yeast, a model system used for studying heterochromatin mechanisms because of its comparative simplicity, the precise pattern of methylation depends on a process called RNA interference, or RNAi. It involves a host of players: the enzyme that copies DNA into RNA, which is diced into short segments called short interfering RNAs, or siRNAs; a part of the RNAi machinery known as the RITS complex; and various enzymes that are able to alter the configuration of chromatin.

A debate over recruitment

"In trying to understand the interplay between each of these components," explains Joshua-Tor, "there has been a longstanding debate over how the RITS complex initially gets recruited to the regions at the centromere that are destined to become heterochromatin."

At first, scientists thought that the siRNA molecules acted as guides to recruit RITS. After latching on to the chromatin, RITS was in turn thought to recruit the other components: the enzyme that adds the methyl marks; and the protein Chp1, which acts as a molecular "velcro" to keep the RITS complex firmly attached to the methyl-decorated chromatin.

The importance of binding strength

The CSHL team in collaboration with the team of Janet Partridge at St. Jude's Children's Research Hospital, Memphis, has now found that siRNAs cannot do the job of heterochromatin assembly by themselves. Rather, the siRNA-guided interaction relies on the strength with
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Contact: Hema Bashyam
bashyam@cshl.edu
516-367-6822
Cold Spring Harbor Laboratory
Source:Eurekalert

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