For the study, Dominski adapted a laboratory system that reproduces in the test tube what normally occurs in the cell when FLASH participates in the biochemical cleavage event that results in mature histone messenger RNA. This enabled his team to explore what might occur when FLASH was added or removed.

"We could then figure out exactly what portion of FLASH would restore the protein's function in generating histone mRNAs and remarkably, only the first 100 or so amino acids are required. The remaining 2,000 amino acids of this large protein likely control other processes in the cell, including apoptosis and DNA replication," he explained.

Co-author William F. Marzluff, Ph.D., is distinguished professor of biochemistry and biophysics and executive associate dean for basic research in the UNC School of Medicine. He noted that FLASH is the first component found in this protein complex "that integrates or initiates many cellular functions - DNA replication, apoptosis, histone production. Having this small piece of the puzzle makes it a lot easier to identify others."

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