Title [Minireview]Cytoplasmic molecular chaperones in Pseudomonas species
Author Hyunhee Kim1, Seongjoon Moon1, Soojeong Ham1, Kihyun Lee2, Ute Römling3, and Changhan Lee1*
Address 1Department of Biological Sciences, Ajou University, Suwon 16499, Republic of Korea, 2CJ Bioscience, Seoul 04527, Republic of Korea , 3Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Stockholm 171 77, Sweden
Bibliography Journal of Microbiology, 60(11),1049-1060, 2022,
DOI 10.1007/s12275-022-2425-0
Key Words Pseudomonas, molecular chaperone, protein homeostasis, Pseudomonas aeruginosa, Pseudomonas putida, Pseudomonas syringae, Pseudomonas antarctica, Pseudomonas thermotolerans
Abstract Pseudomonas is widespread in various environmental and host niches. To promote rejuvenation, cellular protein homeostasis must be finely tuned in response to diverse stresses, such as extremely high and low temperatures, oxidative stress, and desiccation, which can result in protein homeostasis imbalance. Molecular chaperones function as key components that aid protein folding and prevent protein denaturation. Pseudomonas, an ecologically important bacterial genus, includes human and plant pathogens as well as growth-promoting symbionts and species useful for bioremediation. In this review, we focus on protein quality control systems, particularly molecular chaperones, in ecologically diverse species of Pseudomonas, including the opportunistic human pathogen Pseudomonas aeruginosa, the plant pathogen Pseudomonas syringae, the soil species Pseudomonas putida, and the psychrophilic Pseudomonas antarctica.