Human NAA30 can rescue yeast mak3∆ mutant growth phenotypes.
MAK3
N-terminal acetylation
NAA30
Saccharomyces cerevisiae
acetyltransferase
stress response
Journal
Bioscience reports
ISSN: 1573-4935
Titre abrégé: Biosci Rep
Pays: England
ID NLM: 8102797
Informations de publication
Date de publication:
26 03 2021
26 03 2021
Historique:
received:
14
08
2020
revised:
08
02
2021
accepted:
16
02
2021
pubmed:
19
2
2021
medline:
24
12
2021
entrez:
18
2
2021
Statut:
ppublish
Résumé
N-terminal acetylation is an irreversible protein modification that primarily occurs co-translationally, and is catalyzed by a highly conserved family of N-terminal acetyltransferases (NATs). The NatC complex (NAA30-NAA35-NAA38) is a major NAT enzyme, which was first described in yeast and estimated to N-terminally acetylate ∼20% of the proteome. The activity of NatC is crucial for the correct functioning of its substrates, which include translocation to the Golgi apparatus, the inner nuclear membrane as well as proper mitochondrial function. We show in comparative viability and growth assays that yeast cells lacking MAK3/NAA30 grow poorly in non-fermentable carbon sources and other stress conditions. By using two different experimental approaches and two yeast strains, we show that liquid growth assays are the method of choice when analyzing subtle growth defects, keeping loss of information to a minimum. We further demonstrate that human NAA30 can functionally replace yeast MAK3/NAA30. However, this depends on the genetic background of the yeast strain. These findings indicate that the function of MAK3/NAA30 is evolutionarily conserved from yeast to human. Our yeast system provides a powerful approach to study potential human NAA30 variants using a high-throughput liquid growth assay with various stress conditions.
Identifiants
pubmed: 33600573
pii: 227865
doi: 10.1042/BSR20202828
pmc: PMC7938456
pii:
doi:
Substances chimiques
Saccharomyces cerevisiae Proteins
0
MAK3 protein, S cerevisiae
EC 2.3.1.256
N-Terminal Acetyltransferase C
EC 2.3.1.256
NAA30 protein, human
EC 2.3.1.256
Arylamine N-Acetyltransferase
EC 2.3.1.5
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© 2021 The Author(s).
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