What is it about?
Retrovirus-like retrotransposons influence genome evolution of their hosts and replicate within cytoplasmic particles. How their building blocks associate and assemble within the cell is poorly understood. We discovered a prion-like domain (PrLD) in the budding yeast retrotransposon Ty1 Gag protein that builds virus-like particles. The PrLD has similar sequence properties to prions and disordered protein domains that can drive the formation of assemblies that range from liquid to solid. We demonstrate that the Ty1 PrLD can function as a prion and that certain prion sequences can replace the PrLD and support Ty1 transposition.
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Why is it important?
Our work bridges a continuum between disordered protein domains, prion function, and virus assembly. In addition, the system we developed is an effective plug-and-play platform that should be useful for characterizing disordered sequences in living cells.
Perspectives
The work was originally conceived when Sean Beckwith identified the prion-like domain in a retrovirus-like transposon using computational approaches that matured into a story rich with biological significance.
David J. Garfinkel
University of Georgia
Read the Original
This page is a summary of: An interchangeable prion-like domain is required for Ty1 retrotransposition, Proceedings of the National Academy of Sciences, July 2023, Proceedings of the National Academy of Sciences,
DOI: 10.1073/pnas.2303358120.
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