Trehalose protects Escherichia coli against carbon stress manifested by protein acetylation and aggregation
Maria Moruno Algara , Dorota Kuczyńska-Wiśnik , Janusz Dębski , Karolina Stojowska-Swędrzyńska , Hanna Sominka , Małgorzata Bukrejewska , Ewa Laskowska
AbstractThe 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 coliΔotsA cells, which are unable to synthesize trehalose, the aggregation of endog-enous 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 proteosta-sis 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.
|Journal series||Molecular Microbiology, ISSN 0950-382X, (N/A 100 pkt)|
|Publication size in sheets||0.7|
|Score||= 100.0, 28-01-2020, ArticleFromJournal|
|Publication indicators||: 2017 = 1.043; : 2018 = 3.649 (2) - 2018=3.819 (5)|
|Citation count*||1 (2020-03-20)|
* presented citation count is obtained through Internet information analysis and it is close to the number calculated by the Publish or Perish system.