Regulation of Septin Dynamics by the Saccharomyces cerevisiae Lysine Acetyltransferase NuA4
Author Information
Author(s): Mitchell Leslie Lau, André Lambert, Jean-Philippe Zhou, Hu Fong Ying Couture, Jean-François Figeys, Daniel Baetz, Kristin Hardwick
Primary Institution: Ottawa Institute of Systems Biology, Department of Biochemistry, Microbiology, and Immunology, University of Ottawa, Ottawa, Ontario, Canada
Hypothesis
NuA4 regulates septin dynamics through the acetylation of septin proteins.
Conclusion
The study provides evidence that NuA4 impacts septin dynamics and identifies acetylation as a novel post-translational modification regulating septin proteins.
Supporting Evidence
- NuA4 is linked to various cellular processes through the acetylation of histone and non-histone targets.
- Genome-wide SDL screens identified a novel connection between NuA4 and septin proteins.
- Acetylation levels of septin proteins are reduced in catalytically inactive NuA4 mutants.
- Cells expressing a Shs1 protein with decreased acetylation have defects in septin localization.
Takeaway
This research shows that a specific protein complex in yeast helps control how another group of proteins, called septins, behave during cell division.
Methodology
The study utilized genome-wide synthetic dosage lethal screens to identify genetic interactions and assess the role of NuA4 in septin dynamics.
Digital Object Identifier (DOI)
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