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Crystal Structure Of The Archaeal Chaperonin Thermosome, A Protein-Folding Machine, Determined

A research team at the Max Planck Institute of Biochemistry , Martinsried/Germany, and the Institute of Microbiology, University of Regensburg, has solved the crystal structure of the thermosome. This structure, published in Cell on April 3, 1998, provides clues for understanding the mode of action of archaeal and eukaryotic chaperonins.

Proteins require a defined three-dimensional structure to fulfill central tasks in living organisms. Protein folding - the process in which they acquire their native structure - has been recognized as a spontaneous process. The three-dimensional structure is coded in the sequence of the building blocks, the amino acid. However, in the cellular environment proteins have to adopt their structure in a very short time after synthesis in the presence of a large number of other cellular components that could interfere with this process. Therefore a class of proteins, the chaperones, has evolved that rescues the folding intermediates from aggregation. A special kind of chaperones are double-ring, oligomeric containers, termed chaperonins. They provide closed compartments that shield folding proteins from the cellular environment.

According to their general importance chaperonins are present in all three kingdoms of life: eubacteria, archaea and eukaryotes. Based on their evolutionary relationship they fall into two distinct groups. The prototype of group I chaperonins is represented by GroEL which occurs in the eubacterium Escherichia coli. Group II chaperonins are comprised of the archaeal chaperonins, e.g. the thermosome of the present study, and the eukayotic CCT which occurs in higher organisms as human beings.

Members of both groups consume energy to drive the folding cycle by hydrolyzing ATP and share a basic principle of action. However, the implementation at th
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Contact: Robert Huber
huber@biochem.mpg.de
+49-89-85782678
Max-Planck-Gesellschaft
3-Apr-1998


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