In the study, published in the April 7 issue of the journal Molecular Cell, researchers Sean Studer and Simpson Joseph in UCSD's Department of Chemistry and Biochemistry report how the messenger RNA instructions to make a protein are unfolded in a bacterial cell, so that they can be read by the cell's protein-making machinery. Since unfolding the instructions is an essential step in the making of a protein, the researchers say that drugs designed to interfere with this step would make ideal antibiotics.
"With antibiotic-resistant strains of bacteria on the rise, there is a crisis in the management and treatment of these infections throughout the world," said Simpson Joseph, a professor of chemistry and biochemistry who led the study. "Our results will provide insights for developing novel antibiotics that target the messenger RNA unfolding process in disease-causing bacteria."
Messenger RNA (mRNA) feeds through a ribosome--protein factory in a cell--like a tape through a teletype machine. There the RNA instructions are read and a protein is assembled, one amino acid building block at a time. However, mRNA is usually folded up like origami. Until now, scientists did not understand how the mRNA in bacteria was unfolded so it could be read by the ribosome.
"It's been known for about 10 years that in humans and other complex organisms there is a specialized unwinding mechanism that requires a number of different proteins working in cooperation," explained Sean Studer, a chemistry and biochemistry graduate student who conducted the research. "But the process is not the same in bacteria, and while there is a great deal of research on protein synthesis in bacteria, the unfolding step is one aspect that has been overlooked."