RNA Puts Proteins in a Headlock

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

Written byKerry Grens
| 1 min read

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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 ...

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  • kerry grens

    Kerry served as The Scientist’s news director until 2021. Before joining The Scientist in 2013, she was a stringer for Reuters Health, the senior health and science reporter at WHYY in Philadelphia, and the health and science reporter at New Hampshire Public Radio. Kerry got her start in journalism as a AAAS Mass Media fellow at KUNC in Colorado. She has a master’s in biological sciences from Stanford University and a biology degree from Loyola University Chicago.

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