Role of Apis cerana cerana N-terminal asparagine amidohydrolase (AccNtan1) in 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
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

337-348

Informations de copyright

© The Author(s) 2020. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Auteurs

Guangdong Zhao (G)

State Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Daizong Road No.61, Taian, Shandong 271018, PR China.

Chen Wang (C)

State Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Daizong Road No.61, Taian, Shandong 271018, PR China.

Ying Wang (Y)

College of Animal Science and Technology, Shandong Agricultural University, Daizong Road No.61, Taian, Shandong 271018, PR China.

Lijun Wang (L)

State Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Daizong Road No.61, Taian, Shandong 271018, PR China.

Baohua Xu (B)

College of Animal Science and Technology, Shandong Agricultural University, Daizong Road No.61, Taian, Shandong 271018, PR China.

Xingqi Guo (X)

State Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Daizong Road No.61, Taian, Shandong 271018, PR China.

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Classifications MeSH