Research

 

Associate Professor of Biology Emily Wiley publishes article titled Phosphorylation-dependent targeting of Tetrahymena HP1 to condensed chromatin.
Emily Wiley
9/10/2016
 
 
Yale, K., Neuman, M., Bulley, E., Tackett, A., Chait, B.T., *Wiley, E.A. (2016) Phosphorylation-dependent targeting of Tetrahymena HP1 to condensed chromatin. mSphere 4.
Compacting the genome to various degrees influences processes that use DNA as a template, such as gene transcription and replication. This project was aimed at learning more about the cellular mechanisms that control genome compaction. Posttranslational modifications (PTMs) of proteins involved in genome condensation are emerging as potentially important points of regulation. To help elucidate protein modifications their effects on proteins involved in genome condensation, we investigated the phosphorylation of the chromatin protein called Hhp1 in the ciliated protozoan Tetrahymena thermophila. We found that phosphorylation adjacent to a domain that binds histone H3 was critical for Hhp1 localization to highly condensed regions of "heterochromatin". This is one of the first functional investigations of PTMs on a non-histone chromatin protein that acts on the ciliate genome, and these discoveries should aid in identifying common evolutionarily conserved strategies that control the dynamic compaction of genomes. Most of the work was done by three undergraduates: Katerina Yale (CMC, '12); Monica Neuman (CMC '11) and Emily Bulley (SCR '13).
 
http://msphere.asm.org/content/1/4/e00142-16  

 

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