Components of RNA Activation Complex Identified

These findings were reported in the September 19, 2002, issue of Nature.

While studying the embryonic development of C elegans, researchers from the University of Wisconsin (Madison, USA) observed two proteins, GLD-2 and GLD-3, that when combined formed an enzyme that was able to activate specific RNA molecules outside the nucleus. GLD-2 was found to contain an active site where reactions could take place, but this protein did not bind to RNA. GLD-3 behaved in the opposite fashion: it could bind to RNA but had no active site. Binding the two proteins together created an enzyme that could not only attach itself to RNA but could also chemically modify the RNA in a specific way that activates it.

"One of the big questions in molecular biology is how genes are controlled,” explained senior author Dr. Judith Kimble, professor of biochemistry at the University of Wisconsin. "Our finding provides an important piece of the puzzle.”

Identification of this enzyme in C elegans should promote the search for similar enzymes in humans, possibly one day leading to new therapies. Said Dr. Kimble, "I think this is a big finding for anyone interested in how genes are regulated.”




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