A mutation that frustrates DNA repair likely contributes to Fanconi anemia
After more than a century of technological refinements, zippers still get stuck. So do the molecular machines that routinely unzip the double helix of DNA in our cells after billions of years of evolution, and the results can be lethal.
In research to be published July 30 in Molecular Cell and already available online, scientists at Rockefeller University and colleagues show how a previously uncharacterized protein associated with the cancer-causing disorder Fanconi anemia might aid in repairing the broken zippers in our genes. When two strands of DNA remain stuck together, they supposed to make. This sticking point is one of the most deadly genetic perils, called an inter-strand crosslink, which threatens an average cell about 10 times a day.
“Repairing the inter-strand crosslink is a very complicated process,” says Agata Smogorzewska, head of the Laboratory of Genome Maintenance at Rockefeller, who led the research. “It takes lots of players, and if they don’t work correctly, the consequences can be terrible.” Thirteen proteins are known to be involved in the Fanconi anemia pathway, which repairs inter-strand crosslinks. If any one of them is damaged, the result is Fanconi anemia, a disorder that leads to bone marrow failure and leukemia, among other cancers, as well as many developmental abnormalities.
Read more here/Leia mais aqui:
Molecular Cell, Volume 39, Issue 1, 36-47, 9 July 2010 | Copyright © 2010 Elsevier Inc. All rights reserved. | 10.1016/j.molcel.2010.06.023
A Genetic Screen Identifies FAN1, a Fanconi Anemia-Associated Nuclease Necessary for DNA Interstrand Crosslink Repair
Vote neste blog para o prêmio TOPBLOG 2010.