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CSHL team solves a protein complex's molecular structure to explain its role in gene silencing
Date:11/13/2011

ua-Tor. For the last few years, her team has explored these questions in fission yeast.

In the current study, the combined use of X-ray crystallography and biochemisty by Research Investigator Thomas Schalch, Ph.D., has yielded a much better picture and revealed further details of how Chp1 interacts with the Tas3 protein. These experiments have also identified a previously unknown substructure at the very end of Chp1.

A clue about what role this structure, called the PIN domain, might play in heterochromatin assembly came from scouring a protein database. The team found that other proteins that had similar structural features were associated with telomeres, the cap-like structures at the end of chromosomes. In fission yeast, telomeres are one of the locations where heterochromatin is found, another being the centromere -- the dense knob-like structure at the center of a chromosome.

The team found that deleting the PIN domain from Chp1 prevented heterochromatin formation at the telomeres but didn't affect formation at the centromere. "This suggests different functions of RITS proteins at centromeres vs telomeres," says Joshua-Tor. "RITS might be exerting its effect at centromeres through Ago1 and the RNAi machinery, but might enforcing its function at the telomeres through Chp1 and its PIN domain." The team is now turning its focus to understanding how these various functions are regulated.


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Contact: Hema Bashyam
bashyam@cshl.edu
516-367-6822
Cold Spring Harbor Laboratory
Source:Eurekalert

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