What is it about?

Almost all sequenced eukaryotes have LisH-containing proteins, which range in function from transcriptional regulators to cytoskeletal remodelers. Although this had not been previously characterized as a repression domain, we found repressive function to be conserved across LisH-Helix1 sequences representing over one thousand different eukaryotic proteins.

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Why is it important?

This work suggests the existence of a novel conserved mechanism for transcriptional repression. Many LisH-containing proteins previously unrecognized as having roles in transcriptional regulation might be repressors in their native contexts. From a synthetic biology perspective, this is the smallest autonomous repression motif described, and can be used as a repressive tag in eukaryotes.


Our work in this paper opens the door for many lines of research. We need to better understand the mechanism by which this motif can repress transcription. We also need to further develop and test this as a tag for transcriptional repression outside of tobacco and yeast. Finally, our work on LisH domains in oncogenes should be studied further to learn of therapeutic applications.

Roman Ramos Baez
University of Chicago

Read the Original

This page is a summary of: A single helix repression domain is functional across diverse eukaryotes, Proceedings of the National Academy of Sciences, October 2022, Proceedings of the National Academy of Sciences,
DOI: 10.1073/pnas.2206986119.
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