Scientific research requires patience. The rewards are not always immediate, and the technology needed does not always exist. Michael A. Trakselis, Ph.D., professor and director of graduate affairs for the Department of Chemistry and Biochemistry at Baylor University, understands this.
For 15 years, Trakselis has been interested in the MCM8/9 enzyme. Part of the minichromosome maintenance protein (MCM) family, MCM8/9 is directly linked to ovarian insufficiency, infertility and cancers including ovarian, testicular and colon cancers, yet little is known about how this enzyme works and its connection to disease. There was no understanding of the relationship between the structure and function of the enzyme.
The research—Activity, substrate preference, and structure of HsMCM8/9 helicase—was published in the journal Nucleic Acids Research. With this new information, researchers in the Trakselis Laboratory and elsewhere have a roadmap to better understand the function of this enzyme complex and how mutations may be connected to disease.
“Mutations in MCM8 or MCM9 can cause infertility and cancer; yet, we don’t know why we get certain diseases when there are mutations in this protein,” Trakselis said. “Having the structure might help us figure out some of that.”
Before that could happen, Trakselis had to overcome