Human N-Alpha-Acetyltransferase 40 Conserved from Yeast Acetylates Histones H2A and H4
Author Information
Author(s): Kristine Hole, Petra Van Damme, Monica Dalva, Henriette Aksnes, Nina Glomnes, Jan Erik Varhaug, Johan R. Lillehaug, Kris Gevaert, Thomas Arnesen
Primary Institution: Department of Molecular Biology, University of Bergen, Bergen, Norway
Hypothesis
The study aims to identify and characterize the human N-Alpha-Acetyltransferase 40 (hNaa40p/hNatD) and its role in acetylating histones H2A and H4.
Conclusion
The results suggest that human Naa40p/NatD is conserved from yeast and specifically acetylates histones H2A and H4.
Supporting Evidence
- Recombinant hNaa40p was shown to acetylate synthetic peptides derived from histones H2A and H4 in vitro.
- Heterologous expression of hNaa40p in yeast restored the acetylation of histone H4.
- Endogenous hNaa40p was found to associate with ribosomes, indicating a co-translational activity.
Takeaway
This study found that a protein called hNaa40p helps add a special tag to two important proteins in our cells, which is similar to what a related protein does in yeast.
Methodology
The study used in vitro assays with recombinant hNaa40p to assess its acetylation activity on histone peptides and heterologous expression in yeast to evaluate its function in vivo.
Limitations
The study does not explore the full range of potential substrates for hNaa40p beyond histones H2A and H4.
Statistical Information
P-Value
0.0104
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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