Role of Apis cerana cerana N-terminal asparagine amidohydrolase (AccNtan1) in oxidative stress.
Apis cerana cerana
N-terminal asparagine amidohydrolase
RNA inference
environmental stress
oxidative stress
Journal
Journal of biochemistry
ISSN: 1756-2651
Titre abrégé: J Biochem
Pays: England
ID NLM: 0376600
Informations de publication
Date de publication:
01 Oct 2020
01 Oct 2020
Historique:
received:
13
10
2019
accepted:
26
02
2020
pubmed:
3
7
2020
medline:
4
3
2021
entrez:
3
7
2020
Statut:
ppublish
Résumé
N-Terminal asparagine amidohydrolase is a component of the ubiquitin-dependent N-end rule pathway of protein degradation that has been implicated in a variety of physiological functions, including the sensing of heme, oxygen, nitric oxide, selective elimination of misfolded proteins and the repair of DNA. We identified the Apis cerana cerana N-terminal asparagine amidohydrolase (AccNtan1) gene from A. cerana cerana and investigated its role in oxidation resistance. Multiple sequence alignments and phylogenetic analysis revealed that N-terminal asparagine amidohydrolase is highly conserved in insect species. Quantitative real-time polymerase chain reaction analysis indicated that the expression levels of AccNtan1 were significantly lower in the wing, honey sac and abdomen than in other tissues and were significantly higher in early stages of development, including the larva, prepupa and pink-eyed pupa stages, than in later stages. We further observed that AccNtan1 expression was induced by several environmental stressors, including aberrant temperature, H2O2, UV, heavy metals and pesticides. Moreover, a bacteriostatic assay suggested that overexpression of AccNtan1 enhances the resistance of bacteria to oxidative stress. In addition, knockdown of AccNtan1 using RNA interference significantly affected the expression levels of most antioxidant genes and the activity levels of several antioxidant enzymes. Thus, we hypothesize that AccNtan1 plays important roles in environmental stress responses and antioxidative processes.
Identifiants
pubmed: 32614443
pii: 5866554
doi: 10.1093/jb/mvaa071
doi:
Substances chimiques
Antioxidants
0
Insect Proteins
0
Amidohydrolases
EC 3.5.-
N-terminal asparagine amidohydrolase
EC 3.5.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
337-348Informations de copyright
© The Author(s) 2020. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.