Epigenetic memory is governed by an effector recruitment specificity toggle in Heterochromatin Protein 1

Amanda Ames, Melissa Seman, Ajay Larkin, Gulzhan Raiymbek, Ziyuan Chen, Alex Levashkevich, Bokyung Kim, Julie Suzanne Biteen and Kaushik Ragunathan ()
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Amanda Ames: Brandeis University
Melissa Seman: Brandeis University
Ajay Larkin: Brandeis University
Gulzhan Raiymbek: University of Michigan
Ziyuan Chen: University of Michigan
Alex Levashkevich: Brandeis University
Bokyung Kim: Brandeis University
Julie Suzanne Biteen: University of Michigan
Kaushik Ragunathan: Brandeis University

Nature Communications, 2024, vol. 15, issue 1, 1-17

Abstract: Abstract HP1 proteins are essential for establishing and maintaining transcriptionally silent heterochromatin. They dimerize, forming a binding interface to recruit diverse chromatin-associated factors. Although HP1 proteins are known to rapidly evolve, the extent of variation required to achieve functional specialization is unknown. To investigate how changes in amino acid sequence impacts heterochromatin formation, we performed a targeted mutagenesis screen of the S. pombe HP1 homolog, Swi6. Substitutions within an auxiliary surface adjacent to the HP1 dimerization interface produce Swi6 variants with divergent maintenance properties. Remarkably, substitutions at a single amino acid position lead to the persistent gain or loss of epigenetic inheritance. These substitutions increase Swi6 chromatin occupancy in vivo and altered Swi6-protein interactions that reprogram H3K9me maintenance. We show how relatively minor changes in Swi6 amino acid composition in an auxiliary surface can lead to profound changes in epigenetic inheritance providing a redundant mechanism to evolve HP1-effector specificity.

Date: 2024
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DOI: 10.1038/s41467-024-50538-z

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