Cold-adapted characteristics and gene knockout of alkyl hydroperoxide reductase subunit C in Antarctic Psychrobacter sp. ANT206.
Alkyl hydroperoxide reductase subunit C
Antarctic
Cold-adaptation
Gene knockout
Molecular dynamics simulation
Journal
World journal of microbiology & biotechnology
ISSN: 1573-0972
Titre abrégé: World J Microbiol Biotechnol
Pays: Germany
ID NLM: 9012472
Informations de publication
Date de publication:
21 Oct 2024
21 Oct 2024
Historique:
received:
10
08
2024
accepted:
07
10
2024
medline:
21
10
2024
pubmed:
21
10
2024
entrez:
21
10
2024
Statut:
epublish
Résumé
Alkyl hydroperoxide reductase subunit C (AhpC) contributes to the cellular defense against reactive oxygen species. However, it remains understudied in psychrophiles. Amino acid comparison demonstrated that AhpC from Psychrobacter sp. ANT206 (ANT206) (PsAhpC) revealed fewer numbers of Lys and more numbers of Gly, which might have favored higher flexibility at low temperature. The recombinant PsAhpC (rPsAhpC) was most active at 25 °C and retained 35% of its residual activity at 0 °C, indicating that it was a cold-adapted enzyme. Additionally, rPsAhpC demonstrated significant salt tolerance, sustaining its activity in the presence of 4.0 M NaCl. Molecular dynamics simulations indicated that PsAhpC had comparatively loose conformation, which facilitated reactions at low temperatures. Subsequently, an ahpc knockout mutant was constructed, and the growth rate of the knockout mutant significantly decreased, suggesting that ahpc might be crucial for the growth of ANT206 at low temperatures. The findings provide a robust foundation for further investigation into the structural features and catalytic characterization of cold-adapted AhpC. The structural characteristics of PsAhpC and its cold tolerance and salt tolerance may be applied to stress resistance breeding of various organisms.
Identifiants
pubmed: 39432194
doi: 10.1007/s11274-024-04158-w
pii: 10.1007/s11274-024-04158-w
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
359Subventions
Organisme : Natural Science Foundation of Shandong Province
ID : ZR2021MD040
Organisme : Natural Science Foundation of Shandong Province
ID : ZR2023QD126
Organisme : he project of 'Double first-class' discipline construction fund
ID : 2023SYLHY17
Organisme : Fundamental Research Funds for the Central Universities
ID : HIT.DZJJ.2023151
Organisme : National Natural Science Foundation of China
ID : 41876149
Organisme : The project of 'Double first-class' discipline construction fund
ID : 2023SYLHY08
Organisme : 2023 Harbin Institute of Technology Weihai Campus Teaching Reform Research Project
ID : 2023MSZZ03
Informations de copyright
© 2024. The Author(s), under exclusive licence to Springer Nature B.V.
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