Johns Hopkins Scientists Discover Protein 'Lynchpin'

A pioneering view of the internal structure of RNA captured by scientists at The Johns Hopkins University will become public today in a report published by the journal "Science."

The work of an interdisciplinary team of chemists and biophysicists marks the first actual atomic level resolution of a protein-RNA complex from the ribosome ever to be produced and only the third RNA ever to have its complex higher-order construction revealed.

"I've been traveling around the last few weeks giving talks about what we've discovered," said chemistry professor David Draper, out of whose lab the work originated, "and people's jaws just drop to the floor. So little has been known about how RNAs fit together and what kinds of structural features keep it intact. Well, now we can actually see it in 3-D, living color."

The detailed structure is significant because so little is known about it. Also, RNA's stature has risen extraordinarily in the past two decades with discoveries that RNA not only carries the genetic blueprint to the ribosomes for protein encoding, but also serves as the catalyst that carries out the reactions and does the major work of the ribosome. Its ability to both store genetic information and catalyze biological reactions identifies it as central to the origins of life and suggests that it is critical for the regulation of genes and pathogens.

Unfortunately, scientists still have only a primitive understanding of RNA. Its many entwined helical elements are tightly packed into an extremely complicated, globular structure, making even a simple viewing a difficult biophysical adventure.

By binding a particularly stable kind of protein commonly known as L11 to RNA synthesized in the lab, Draper's group created an RNA-protein complex that was at last robust enough to withstand the rigors of analysis--in this case, c
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Contact: Gary Dorsey
gdd@jhu.edu
410-516-7906
Johns Hopkins University
14-May-1999