Extended N-Terminal Acetyltransferase Naa50 in Filamentous Fungi Adds to Naa50 Diversity.
Chaetomium thermophilum
GNAT domain
N-terminal acetyltransferase
NAT
Naa50
NatE
Neurospora crassa
X-ray structure
dynein light chain protein 1
ribosome association
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
16 Sep 2022
16 Sep 2022
Historique:
received:
05
08
2022
revised:
09
09
2022
accepted:
13
09
2022
entrez:
23
9
2022
pubmed:
24
9
2022
medline:
28
9
2022
Statut:
epublish
Résumé
Most eukaryotic proteins are N-terminally acetylated by a set of Nα acetyltransferases (NATs). This ancient and ubiquitous modification plays a fundamental role in protein homeostasis, while mutations are linked to human diseases and phenotypic defects. In particular, Naa50 features species-specific differences, as it is inactive in yeast but active in higher eukaryotes. Together with NatA, it engages in NatE complex formation for cotranslational acetylation. Here, we report Naa50 homologs from the filamentous fungi
Identifiants
pubmed: 36142717
pii: ijms231810805
doi: 10.3390/ijms231810805
pmc: PMC9500918
pii:
doi:
Substances chimiques
Acetyltransferases
EC 2.3.1.-
N-Terminal Acetyltransferase E
EC 2.3.1.258
N-Terminal Acetyltransferases
EC 2.3.1.88
Dyneins
EC 3.6.4.2
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Deutsche Forschungsgemeinschaft
ID : DFG: SI 586/6-1
Organisme : Deutsche Forschungsgemeinschaft
ID : Project-ID 201348542 - SFB 1036 (TP22)
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