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

NAA10 is a major <i>N</i>-terminal acetyltransferase (NAT) that catalyzes the cotranslational <i>N</i>-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...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Rasmus Ree, Karoline Krogstad, Nina McTiernan, Magnus E. Jakobsson, Thomas Arnesen
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	protein hydroxylation protein acetylation proteomics POST-translational modification <i>N</i>-terminal acetyltransferase NAA10 Biology (General) QH301-705.5 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/21747304c7b14645a8581653b8e78998
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:21747304c7b14645a8581653b8e78998
record_format	dspace
spelling	oai:doaj.org-article:21747304c7b14645a8581653b8e789982021-11-11T17:14:57ZHydroxylation of the Acetyltransferase NAA10 Trp38 Is Not an Enzyme-Switch in Human Cells10.3390/ijms2221118051422-00671661-6596https://doaj.org/article/21747304c7b14645a8581653b8e789982021-10-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/21/11805https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067NAA10 is a major <i>N</i>-terminal acetyltransferase (NAT) that catalyzes the cotranslational <i>N</i>-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.Rasmus ReeKaroline KrogstadNina McTiernanMagnus E. JakobssonThomas ArnesenMDPI AGarticleprotein hydroxylationprotein acetylationproteomicsPOST-translational modification<i>N</i>-terminal acetyltransferaseNAA10Biology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 11805, p 11805 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	protein hydroxylation protein acetylation proteomics POST-translational modification <i>N</i>-terminal acetyltransferase NAA10 Biology (General) QH301-705.5 Chemistry QD1-999
spellingShingle	protein hydroxylation protein acetylation proteomics POST-translational modification <i>N</i>-terminal acetyltransferase NAA10 Biology (General) QH301-705.5 Chemistry QD1-999 Rasmus Ree Karoline Krogstad Nina McTiernan Magnus E. Jakobsson Thomas Arnesen Hydroxylation of the Acetyltransferase NAA10 Trp38 Is Not an Enzyme-Switch in Human Cells
description	NAA10 is a major <i>N</i>-terminal acetyltransferase (NAT) that catalyzes the cotranslational <i>N</i>-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.
format	article
author	Rasmus Ree Karoline Krogstad Nina McTiernan Magnus E. Jakobsson Thomas Arnesen
author_facet	Rasmus Ree Karoline Krogstad Nina McTiernan Magnus E. Jakobsson Thomas Arnesen
author_sort	Rasmus Ree
title	Hydroxylation of the Acetyltransferase NAA10 Trp38 Is Not an Enzyme-Switch in Human Cells
title_short	Hydroxylation of the Acetyltransferase NAA10 Trp38 Is Not an Enzyme-Switch in Human Cells
title_full	Hydroxylation of the Acetyltransferase NAA10 Trp38 Is Not an Enzyme-Switch in Human Cells
title_fullStr	Hydroxylation of the Acetyltransferase NAA10 Trp38 Is Not an Enzyme-Switch in Human Cells
title_full_unstemmed	Hydroxylation of the Acetyltransferase NAA10 Trp38 Is Not an Enzyme-Switch in Human Cells
title_sort	hydroxylation of the acetyltransferase naa10 trp38 is not an enzyme-switch in human cells
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/21747304c7b14645a8581653b8e78998
work_keys_str_mv	AT rasmusree hydroxylationoftheacetyltransferasenaa10trp38isnotanenzymeswitchinhumancells AT karolinekrogstad hydroxylationoftheacetyltransferasenaa10trp38isnotanenzymeswitchinhumancells AT ninamctiernan hydroxylationoftheacetyltransferasenaa10trp38isnotanenzymeswitchinhumancells AT magnusejakobsson hydroxylationoftheacetyltransferasenaa10trp38isnotanenzymeswitchinhumancells AT thomasarnesen hydroxylationoftheacetyltransferasenaa10trp38isnotanenzymeswitchinhumancells
_version_	1718432104807661568

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

Ejemplares similares