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Protein clamps tight to telomeres to help prevent aging...and support cancer
Date:9/15/2010

lts, telomerase is active in stem cells, certain immune system cells and, most notably, cancer cells.

According to Skordalakes, the discovery of the dimeric nature of Cdc13 sheds light into the core function of this protein, the recruitment of telomerase (which is also a dimer) to the telomeres. Within the Cdc13 dimer are multiple sites that can bind to DNA with varying degrees of affinity. This allows Cdc13 to straddle the DNA so that one section grips tightly to DNA, while another section with a more relaxed grip can bind nearer the tail end of the DNA strand and where telomerase binds. This feature of Cdc13 also assists in recruiting telomerase, summoning the enzyme into place above the telomere.

"You can think of Cdc13 as if it were you hanging on to the edge of a cliff, with one grip stronger than the other," Skordalakes said. "You're going to keep that strong hand on the cliff's edge while your weaker hand reaches into your pocket for your phone."

When Cdc13 interacts with telomerase, Skordalakes says, its weaker hand lets go of DNA, allowing the telomerase to access the telomere while the "strong hand" keeps the telomerase-Cdc13 complex firmly attached to the chromosome end. "It effectively serves as both a protective placeholder and a means of guiding telomerase activity," Skordalakes said.

The Skordalakes laboratory continues to explore the complex biology of telomeres, as well as the numerous other proteins necessary for telomere lengthening to occur. Meanwhile, they are investigating the potential of small molecule inhibitors to serve as viable therapeutics against cancer by blocking telomerase and their related proteins.


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Contact: Greg Lester
glester@wistar.org
215-898-3943
The Wistar Institute
Source:Eurekalert

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