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Hydroxylation of the acetyltransferase NAA10 Trp38 is not an enzyme-switch in human cells

Ree, Rasmus ; Krogstad, Karoline ; McTiernan, Nina ; Jakobsson, Magnus E. LU and Arnesen, Thomas (2021) In International Journal of Molecular Sciences 22(21).
Abstract

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... (More)

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.

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author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
N-terminal acetyltransferase, NAA10, POST-translational modification, Protein acetylation, Protein hydroxylation, Proteomics
in
International Journal of Molecular Sciences
volume
22
issue
21
article number
11805
publisher
MDPI AG
external identifiers
  • pmid:34769235
  • scopus:85118114250
ISSN
1661-6596
DOI
10.3390/ijms222111805
language
English
LU publication?
yes
additional info
Publisher Copyright: © 2021 by the authors. Licensee MDPI, Basel, Switzerland.
id
870ddb29-3e31-4719-aaef-6d6c60981692
date added to LUP
2021-11-16 11:08:35
date last changed
2025-01-13 17:42:28
@article{870ddb29-3e31-4719-aaef-6d6c60981692,
  abstract     = {{<p>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.</p>}},
  author       = {{Ree, Rasmus and Krogstad, Karoline and McTiernan, Nina and Jakobsson, Magnus E. and Arnesen, Thomas}},
  issn         = {{1661-6596}},
  keywords     = {{N-terminal acetyltransferase; NAA10; POST-translational modification; Protein acetylation; Protein hydroxylation; Proteomics}},
  language     = {{eng}},
  month        = {{11}},
  number       = {{21}},
  publisher    = {{MDPI AG}},
  series       = {{International Journal of Molecular Sciences}},
  title        = {{Hydroxylation of the acetyltransferase NAA10 Trp38 is not an enzyme-switch in human cells}},
  url          = {{http://dx.doi.org/10.3390/ijms222111805}},
  doi          = {{10.3390/ijms222111805}},
  volume       = {{22}},
  year         = {{2021}},
}