RNA Puts Proteins in a Headlock

A noncoding RNA initiates translation by grabbing hold of repressor proteins and restricting their functions.

By | May 20, 2014

WIKIMEDIA, DR. RICHARD FELDMANNThe small RNA RsmZ is known to sequester proteins that repress translation in bacteria. A study published in Nature this month (May 14), uncovered the sponge-like ability of the RNA to soak up multiple repressor proteins.

Compared to proteins, the structures of RNA and RNA-protein complexes have been more difficult to determine. The authors, based at ETH Zurich, used a protocol, detailed in a separate Nature Communications paper, combining nuclear magnetic resonance (NMR) and electron paramagnetic resonance spectroscopy to determine the structure of the complex. It’s a “very powerful” tool, Hashim Al-Hashimi, a biochemistry professor at Duke University School of Medicine who was not involved in the work, told Chemical & Engineering News.

According to the news report, the researchers used NMR to determine the structure of the RNA bound to a single repressor protein. Pairing that with electron paramagnetic resonance spectroscopy, the researchers ascertained the complete structure of the complex, which illustrated how the various arms of the RNA act in concert. “RNA-protein binding is cooperative—one dimer induces changes to the RNA structure to promote binding of subsequent dimers,” C & E N reported.


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