A team of researchers is being recognized for devising a new way to study a human protein that long has evaded close scrutiny by scientists investigating its role in the communication of important genetic messages inside a cell's nucleus to workhorse molecules found elsewhere.
Last year, the team, led by J. Andrew Hockert, at the time a doctoral researcher at the Texas Tech University Health Science Center School of Medicine, put in its crosshairs the protein known as CstF-64. Today, in what has been named a "Paper of the Week" for the Jan. 1 issue of the Journal of Biological Chemistry, the team is reporting its successes.
Short for "cleavage stimulation factor-64," CstF-64 carries out countless activities required to keep its parent cell alive and well. Hockert's team was particularly interested in the protein because it controls polyadenylation, an essential step in gene communication that involves tacking on information to genetic messages.
For years, CstF-64 refused to give up its secrets when scientists zeroed in. The protein has so many important duties that tweaks prompted a sort of murder-suicide: It killed its own parent cell and, so, died with it.
"Previously, it had been very hard to examine the functions of most of the polyadenylation proteins in cells because polyadenylation is essential for 'life as we know it.' If we perturbed polyadenylation in any way, the cells died, and we could not measure anything," says Hockert, who is now an assistant professor at the University of the Cumberlands in Williamsburg, Ky.
Undeterred, Hockert set out to observe in a living cell how the elusive CstF-64 gets from its home base in the cytoplasm, or outer region of a cell, and into the nucleus, where genetic messages originate.
For CstF-64, it's all about location, location, location. Only once in the nucleus can it start doing its job in the polyadenylation process, getting the messages ready t
|Contact: Angela Hopp|
American Society for Biochemistry and Molecular Biology