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Protein Refolds to Perform Second Job

The transcription factor RfaH unfolds and then refolds into a new conformation to become a translation factor. Ian Chant reports

Secret identities aren’t just for superheroes anymore. Researchers have found that a protein present in everything from amoebas to people is living a double life. Once it binds to DNA, the protein, called RfaH, rips apart—and then refolds into a different shape, to do a different job.

RfaH is a transcription protein—attached to or freed from a stretch of DNA, it determines if a gene is expressed or not. But once the protein has carried out its task, its helical structure unravels. Within seconds, it refolds into a barrel structure, which has a new role, this time in translation, where it helps the cell produce amino acids for new proteins. The study is in the journal Cell. [Björn M. Burmann et al., "An α Helix to β Barrel Domain Switch Transforms the Transcription Factor RfaH into a Translation Factor"]

The next step is to find out if the barrel can refold into the helix. After that, researchers want to see if proteins similar to RfaH—which are present in all life on Earth—are capable of comparable molecular contortion. Which would mean a lot more bang for our protein buck.

—Ian Chant

[The above text is a transcript of this podcast.]

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