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A unique tail at one end of a protein called Ubc12 stabilizes a molecular workshop that assembles a switch that cells can use to accelerate cell replication. This finding by St. Jude investigators is published in Nature Structural and Molecular Biology (NSMB).
The discovery of the exact structure of the tail and its role in cell replication both reveals a fundamental cellular regulatory mechanism and holds promise that researchers can develop new types of drugs targeting that tail or the workshop itself. The St. Jude researchers report that the stabilizing influence of Ubc12’s protein tail is based on its ability to nestle within a groove of the larger molecule called APPBP1-UBA3. These two proteins, also known by the shorthand designation of E2 (Ubc12) and E1 (APPBP1-UBA3), cooperate with each other to form a workshop where a switch that accelerates cell replication is cobbled together.
Until now, the function of the E2 tail was unknown, according to Brenda Schulman, PhD, of Genetics and Tumor Cell Biology and Structural Biology. Schulman is senior author of the NSMB report. “Knowing the exact shape and function of both the E2 tail and the groove along E1 that the tail fits into make these structures potential targets for new drugs,” adds St. Jude postdoctoral fellow Danny Huang, PhD, first author of the paper.
Other St. Jude authors of the paper are Robert Cassell, Hartwell Center; David Miller, of Structural Biology and Genetics and Tumor Cell Biology; and Martine Roussel, PhD, and Rose Mathew, both of Genetics and Tumor Cell Biology.
St. Jude remains on the cutting edge of discovery. The field of ubiquination, which is the subject of these findings, is also the basis for the 2004 Nobel Prize in Chemistry that was announced earlier this week.