Weizmann Scientists Demonstrate Self-Synthesis & Self-Assembly of 30S Subunit of Ribosome

As the cell's protein factory, the ribosome is the only natural machine that manufactures its own parts. That is why understanding how the machine itself is made, could unlock the door to everything from understanding how life develops to designing new methods of drug production. An intensive, long research effort at the Weizmann Institute of Science in Israel has now demonstrated the self-synthesis and assembly of the small subunit of a ribosome-the 30S subunit--on a surface of a chip. Professor Roy Bar-Ziv, PhD, and Staff Scientist Dr. Shirley Shulman Daube, PhD, of the Institute's Chemical and Biological Physics Department have been working on this project for around seven years. One of the main challenges to such a project is the sheer number of different molecules the cell must produce to make the subunit: The core is a long strand of RNA, and 20 different proteins must be attached to the strand. These get organized by the weak chemical forces between the protein molecules and the RNA--repelling at some points and attracting at others--and the whole structure thus relies on the proper manufacture and organization of each component. Add to that another six proteins that are not part of the structure, but act as chaperones to assist in the assembly. That makes at total of a least 27 different genes--one to encode the RNA and each protein component or chaperone--that must work together to make the subunit. Together with postdoctoral fellow Michael Levy, PhD, who led the current study, and research student Reuven Falkovich, the team produced the subunits on tailored chips that Dr. Bar-Ziv has developed in his lab. Ultimately, they succeeded in mimicking the natural process of synthesizing the parts and assembling them into the ribosome subunits.
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