These researchers use photocrosslinking with a genetically encoded unnatural amino acid, pBpa, to capture a transient interaction between VP-16 and Swi/Snf and to determine which regions of those proteins are actually touching. They found that both N and C terminal regions of VP-16 activation domain contact Swi/Snf. They at least make it sound like this is the most transient interaction captured with this method to-date.
Thursday, November 17, 2011
Caught in the Act: Covalent Cross-Linking Captures Activator–Coactivator Interactions in Vivo
These researchers use photocrosslinking with a genetically encoded unnatural amino acid, pBpa, to capture a transient interaction between VP-16 and Swi/Snf and to determine which regions of those proteins are actually touching. They found that both N and C terminal regions of VP-16 activation domain contact Swi/Snf. They at least make it sound like this is the most transient interaction captured with this method to-date.
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This method has to deal with all the complications of unnatural amino acid integration, but I think there is a big pay-off. The transcription factor interactions seem like the perfect system for the photo cross-linkers because of their transient protein-protein interactions. Also, in the same experiment you find out some structural information. I'm not aware of any other method that can tell you structural info for transient interactions...very cool.
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