Cancer catalyst: Three-dimensional structure of the conserved pseudoknot found in human telomerase RNA.
Credit: Juli Feigon/University of California at Los Angeles
Find dubbed 'a breathrough'
"This was really the breakthrough," he said. "Once we found that the gene from this organism expressed the protein in the quantities we needed, we were able to move quickly."
The researchers used a technique called X-ray crystallography that analyses the patterns of X-rays beamed at molecule crystals to create a three-dimensional structure of the enzyme's active region.
Knowing how this region - called the telomerase reverse transcriptase protein (TERT) - is structured made it possible to decipher how the enzyme works.
"For the first time, we can see how telomerase assembles at the end of chromosomes in initiate telomere replication," said Skordalakes.
Several scientists who reviewed the study ahead of publication hailed its significance. They added, though, that it was only one in a series of essential steps that led to any novel treatment for cancer.
"There is no doubt that having determined the structure of telomerase is extremely important in understanding cancer biology, and will probably help lead us in the development of telomerase inhibitors," said Herbie Newell, head of Britain's Translational Research at Cancer Research.
"But whether these inhibitors will ultimately represent an effective class of anti-cancer treatments, it is too early to say," he added.
Jon Wilson, a scientist at the Institute of Cancer Research in London, described the research as a "major breakthrough" in the study of telomeres in the cancer process.
But he, too, cautioned that the development of drugs to deactivate the enzyme "in a therapeutic setting, although an exciting prospect, will require a great deal more research."
