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Article

Hydroxylation of the Acetyltransferase NAA10 Trp38 Is Not an Enzyme-Switch in Human Cells

1
Department of Biomedicine, University of Bergen, Jonas Lies vei 91, 5009 Bergen, Norway
2
Department of Immunotechnology, Lund University, Medicon Village, 22100 Lund, Sweden
3
Department of Biosciences, University of Bergen, 5009 Bergen, Norway
4
Department of Surgery, Haukeland University Hospital, 5021 Bergen, Norway
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Academic Editor: Djuro Josic
Int. J. Mol. Sci. 2021, 22(21), 11805; https://doi.org/10.3390/ijms222111805
Received: 22 September 2021 / Revised: 27 October 2021 / Accepted: 27 October 2021 / Published: 30 October 2021
(This article belongs to the Special Issue Modifications of Protein Termini)
NAA10 is a major N-terminal acetyltransferase (NAT) that catalyzes the cotranslational N-terminal (Nt-) acetylation of 40% of the human proteome. Several reports of lysine acetyltransferase (KAT) activity by NAA10 exist, but others have not been able to find any NAA10-derived KAT activity, the latter of which is supported by structural studies. The KAT activity of NAA10 towards hypoxia-inducible factor 1α (HIF-1α) was recently found to depend on the hydroxylation at Trp38 of NAA10 by factor inhibiting HIF-1α (FIH). In contrast, we could not detect hydroxylation of Trp38 of NAA10 in several human cell lines and found no evidence that NAA10 interacts with or is regulated by FIH. Our data suggest that NAA10 Trp38 hydroxylation is not a switch in human cells and that it alters its catalytic activity from a NAT to a KAT. View Full-Text
Keywords: protein hydroxylation; protein acetylation; proteomics; POST-translational modification; N-terminal acetyltransferase; NAA10 protein hydroxylation; protein acetylation; proteomics; POST-translational modification; N-terminal acetyltransferase; NAA10
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MDPI and ACS Style

Ree, R.; Krogstad, K.; McTiernan, N.; Jakobsson, M.E.; Arnesen, T. Hydroxylation of the Acetyltransferase NAA10 Trp38 Is Not an Enzyme-Switch in Human Cells. Int. J. Mol. Sci. 2021, 22, 11805. https://doi.org/10.3390/ijms222111805

AMA Style

Ree R, Krogstad K, McTiernan N, Jakobsson ME, Arnesen T. Hydroxylation of the Acetyltransferase NAA10 Trp38 Is Not an Enzyme-Switch in Human Cells. International Journal of Molecular Sciences. 2021; 22(21):11805. https://doi.org/10.3390/ijms222111805

Chicago/Turabian Style

Ree, Rasmus, Karoline Krogstad, Nina McTiernan, Magnus E. Jakobsson, and Thomas Arnesen. 2021. "Hydroxylation of the Acetyltransferase NAA10 Trp38 Is Not an Enzyme-Switch in Human Cells" International Journal of Molecular Sciences 22, no. 21: 11805. https://doi.org/10.3390/ijms222111805

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