Feeding RNAs to a molecular shredder: Scientists unravel the structure of a regulatory protein complex in RNA disposal

The Max Planck scientists have now elucidated the atomic structure and the operating mechanism of a protein complex (Ski complex) which is involved in the activation of the cytoplasmic Exosome. The Ski complex contains several subunits and can be found in all eukaryotes -- from yeast to humans. "We could show that the Ski complex and the Exosome interact directly and that they jointly form a channel for the RNA which is supposed to be degraded," says Felix Halbach. Like DNA, RNA molecules are often folded. To be degraded by the Exosome, RNA molecules have to be unfolded first -- this task is executed by the Ski complex. The unfolded RNA molecules can then be guided through the joint channel to the Exosome. "The Ski complex feeds RNA molecules to the Exosome," explains the biochemist.

The results also reveal additional parallels between the Exosome and the Proteasome. The Proteasome is the protein complex responsible for the degradation of proteins in a cell. "It becomes clear that these two complexes are not only structurally and functionally similar," says Elena Conti, "also their regulatory subunits work in a similar manner." They unwind RNA molecules or, respectively, proteins and guide them to the active centers of the specific degradation machinery.