Active role of the protein translation machinery in protecting against stress tolerance in Synechococcus elongatus PCC7942.

Cyanobacteria Elongation factor G Protective effects Stress Synechococcus

Journal

Archives of biochemistry and biophysics
ISSN: 1096-0384
Titre abrégé: Arch Biochem Biophys
Pays: United States
ID NLM: 0372430

Informations de publication

Date de publication:
15 09 2023
Historique:
received: 01 11 2022
revised: 11 07 2023
accepted: 27 08 2023
medline: 18 9 2023
pubmed: 31 8 2023
entrez: 30 8 2023
Statut: ppublish

Résumé

In vivo protein synthesis is crucial for all domains of life. It is accomplished through translational machinery, and a key step is the translocation of tRNA-mRNA by elongation factor G (EF-G). Genome-based analysis revealed two EF-G encoding genes (S0885 and S2082) in the freshwater cyanobacterium model Synechococcus elongatus PCC7942. S0885 is the essential EF-G gene for photosynthesis. We generated a strain of S. elongatus PCC7942 that overexpressed S0885 (OX-S0885) to identify EF-G functionality. RT-PCR and Western blot analyses revealed increased transcriptional and translational levels in OX-S0885 at 10.5-13.5 and 2.0-3.0 fold, respectively. Overexpression of S0885 led to an increase in specific growth rate. Additionally, polysome-to-monosome ratio (P/M) and RNA-to-protein ratio (R/P) were elevated in OX-S0885 compared with the empty vector. Interestingly, R/P in OX-S0885 was retained at more than 70% under oxidative stress while R/P in the empty vector was severely depleted, suggesting the maintenance of translation. Thus, S0885 appeared to be the important target of oxidative stress because it was protected by the stress response system to maintain its function. These results suggest that cyanobacterial EF-G has a primary function in translation and an unrelated activity during stress conditions. These findings support the substantial role of EF-G in the formation and maintenance of cellular protein formation, and in the protection of the global translational mechanism under oxidative stress condition.

Identifiants

pubmed: 37648010
pii: S0003-9861(23)00233-3
doi: 10.1016/j.abb.2023.109734
pii:
doi:

Substances chimiques

Peptide Elongation Factor G 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

109734

Informations de copyright

Copyright © 2023 Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors declare that they have no conflict of interest.

Auteurs

Siripat Ngoennet (S)

Department of Microbiology, Faculty of Science, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand; Graduate School of Environmental and Human Sciences, Meijo University, Nagoya, Aichi, 468-8502, Japan.

Sophon Sirisattha (S)

Thailand Institute of Scientific and Technological Research (TISTR), Khlong Luang, Pathum Thani, 12120, Thailand.

Pokchut Kusolkumbot (P)

Thailand Institute of Scientific and Technological Research (TISTR), Khlong Luang, Pathum Thani, 12120, Thailand.

Takashi Hibino (T)

Graduate School of Environmental and Human Sciences, Meijo University, Nagoya, Aichi, 468-8502, Japan; Department of Chemistry, Faculty of Science and Technology, Meijo University, Nagoya, Aichi, 468-8502, Japan.

Hakuto Kageyama (H)

Graduate School of Environmental and Human Sciences, Meijo University, Nagoya, Aichi, 468-8502, Japan; Department of Chemistry, Faculty of Science and Technology, Meijo University, Nagoya, Aichi, 468-8502, Japan. Electronic address: kageyama@meijo-u.ac.jp.

Rungaroon Waditee-Sirisattha (R)

Department of Microbiology, Faculty of Science, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand. Electronic address: Rungaroon.W@chula.ac.th.

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Classifications MeSH