Researchers report this week that they are the first to observe the dynamic, ratchet-like movements of single ribosomal molecules in the act of building proteins from genetic blueprints.
Their study, published in the journal Molecular Cell, reveals a key mechanism in the interplay of molecules that allows cells to build the proteins needed to sustain life.
Cells use a variety of tools to build proteins, beginning with messenger RNA, a ribbon-like molecule that codes for the sequence of amino acids in the protein. Another molecule, transfer RNA (tRNA) is uniquely qualified to read this code, but can do so only within the confines of the ribosome. Transfer RNAs bring individual amino acids into the ribosome where they are assembled into proteins. Various other proteins also participate in the process.
When protein translation occurs, single tRNAs enter specific sites in the ribosome, read the code and deliver their amino acids one by one to a growing protein chain. The ribsome transits along the messenger RNA as the protein is built, releasing the "deacylated" tRNA through an exit site.
A ribosome is made up of two subunits composed of ribonucleic acids (RNAs) and about 50 individual proteins.
The ribosome was once considered a static "workbench" for the assembly of new proteins. A recent study by researchers at the Wadsworth Center in Albany, N.Y., using cryo-electron microscopy, showed the ribosomal subunits in two distinct positions relative to one another, however. They proposed that the motion of the subunits depended on a protein catalyst, elongation factor G (EF-G).
In the new study, a team led by University of Illinois physics professor Taekjip Ha used fluorescence resonance energy transfer (FRET) to observe in real time the movement of the ribosomal subunits that is essential for protein synthesis. The team collaborated with Harry Noller, of the University of California at Santa Cruz, who provi
|Contact: Diana Yates|
University of Illinois at Urbana-Champaign