Oct. 25, 2010
NewsScientific News

How to Gum Up the Ribosomal Works

Ribosomes are the protein factories of the cell. Lined up to form veritable assembly lines, these molecular complexes link together the amino-acid building blocks that make up each of the thousands of proteins found in every cell. The heart of the ribosome is the so-called peptidyl transferase center, where the genetic information in the messenger RNA molecule to which the ribosome is attached is translated into the specific sequence of amino acids that forms the corresponding protein. Some mRNA sequences contain signals that cause the process to stall at defined positions. These interruptions play a role in regulating both protein biosynthesis and gene activity. Biochemists led by Dr. Daniel Wilson and Professor Roland Beckmann, both of whom work at LMU's Gene Center and are members of the Excellence Cluster "Center for Integrated Protein Science Munich" (CiPSM), have now elucidated the mechanism that underlies this mode of regulation. "Our findings may some day make it possible to exploit the effect for targeted control of gene activity", says Wilson, "but our immediate priority is to study the termination process in other peptides and other organisms."

Original publication:
Bhushan S. et al.: Structural basis for translational stalling by human cytomegalovirus (hCMV) and fungal arginine attenuator peptide (AAP). Molecular Cell online, issue 40 / 1, p. 138-146, 8 October 2010, DOI:10.1016/j.molcel.2010.09.009



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