Trehalose protects Escherichia coli against carbon stress manifested by protein acetylation and aggregation
| Autor: | Hanna Sominka, Karolina Stojowska-Swędrzyńska, María Moruno Algara, Małgorzata Bukrejewska, Dorota Kuczyńska-Wiśnik, Ewa Laskowska, Janusz Dębski |
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| Rok vydání: | 2019 |
| Předmět: |
Disaccharide
Biology Protein aggregation medicine.disease_cause Microbiology Protein Aggregates 03 medical and health sciences chemistry.chemical_compound Escherichia coli medicine Molecular Biology 030304 developmental biology 0303 health sciences 030306 microbiology Trehalose Acetylation Proteostasis chemistry Biochemistry Glucosyltransferases Mutation Protein stabilization Chemical chaperone |
| Zdroj: | Molecular Microbiology. 112:866-880 |
| ISSN: | 1365-2958 0950-382X |
| DOI: | 10.1111/mmi.14322 |
| Popis: | The disaccharide trehalose is widely distributed in nature and can serve as a carbon reservoir, a signaling molecule for controlling glucose metabolism and a stress protectant. We demonstrated that in Escherichia coli ΔotsA cells, which are unable to synthesize trehalose, the aggregation of endogenous proteins during the stationary phase was increased in comparison to wild-type cells. The lack of trehalose synthesis boosted Nε-lysine acetylation of proteins, which in turn enhanced their hydrophobicity and aggregation. This increased Nε-lysine acetylation could result from carbon overflow and the accumulation of acetyl phosphate caused by the ΔotsA mutation. These findings provide a better understanding of the previously reported protective functions of trehalose in protein stabilization and the prevention of protein aggregation. Our results indicate that trehalose may participate in proteostasis not only as a chemical chaperone but also as a metabolite that indirectly counteracts detrimental protein acetylation. We propose that trehalose protects E. coli against carbon stress - the synthesis and storage of trehalose can prevent carbon overflow, which otherwise is manifested by protein acetylation and aggregation. |
| Databáze: | OpenAIRE |
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