To transcribe the information contained in our genes or to repair the dozens of breaks that occur daily in our DNA, our enzymes must be able to directly access the DNA to perform their functions. However, in the cell nucleus, this access is limited because the DNA strands are often tightly coiled and packed around proteins like threads around spools. Researchers from Lawrence Berkeley National Laboratory (Berkeley Lab), UC Berkeley, the Institute for Systems Biology, and Université Laval now have a better understanding of the protein complex that creates access to packed DNA, TIP60.
Knowing the detailed structure and behavior of TIP60 could provide insight into different diseases where the protein complex plays a role, such as Alzheimer's and various cancers. The work was reported in the journal Science on August 1. This collaborative work brings together structure and functional assays in a powerful way to inform us on how this complex macromolecular assembly carries out its job to regulate the reading of our genome.
The structure of the human TIP60 reveals how evolution has led to the merging of two distinct molecular functions into a single complex, readjusting the way structural modules come together to fit its dual functionality." Eva Nogales, senior faculty scientist at Berkeley Lab, UC Berkeley professor, and Howard Hughes Medical Institute investigator The researchers were able to study the structure of this complex, which is made up of 17 proteins, and the interact.