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

Date:
August 16, 2013
Source:
Max Planck Institute of Biochemistry
Summary:
Any errors that occur during the synthesis of RNA molecules or unwanted accumulation of RNAs can be harmful for the cell. The elimination of defective RNAs or of RNAs that are no longer needed is therefore a key step in the metabolism of a cell.
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The ski complex plays an important role in the quality management of the cell.
Credit: Felix Halbach © MPI of Biochemistry

Any errors that occur during the synthesis of RNA molecules or unwanted accumulation of RNAs can be harmful for the cell. The elimination of defective RNAs or of RNAs that are no longer needed is therefore a key step in the metabolism of a cell. This task is carried out by a protein complex called Exosome, one of the research objects in the department "Structural Cell Biology" headed by Elena Conti. The molecular mechanism of how the Exosome is regulated, however, is not very clear yet.

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.


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The above post is reprinted from materials provided by Max Planck Institute of Biochemistry. Note: Materials may be edited for content and length.


Journal Reference:

  1. Felix Halbach, Peter Reichelt, Michaela Rode, Elena Conti. The Yeast Ski Complex: Crystal Structure and RNA Channeling to the Exosome Complex. Cell, 2013; 154 (4): 814 DOI: 10.1016/j.cell.2013.07.017

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Max Planck Institute of Biochemistry. "Feeding RNAs to a molecular shredder: Scientists unravel the structure of a regulatory protein complex in RNA disposal." ScienceDaily. ScienceDaily, 16 August 2013. <www.sciencedaily.com/releases/2013/08/130816094636.htm>.
Max Planck Institute of Biochemistry. (2013, August 16). Feeding RNAs to a molecular shredder: Scientists unravel the structure of a regulatory protein complex in RNA disposal. ScienceDaily. Retrieved July 28, 2015 from www.sciencedaily.com/releases/2013/08/130816094636.htm
Max Planck Institute of Biochemistry. "Feeding RNAs to a molecular shredder: Scientists unravel the structure of a regulatory protein complex in RNA disposal." ScienceDaily. www.sciencedaily.com/releases/2013/08/130816094636.htm (accessed July 28, 2015).

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