The evolutionarily conserved HtrA is associated with stress tolerance and protein homeostasis in the halotolerant cyanobacterium Halothece sp. PCC7418

• Published in: Extremophiles : life under extreme conditions Vol. 24; no. 3; pp. 377 - 389
• Main Authors: Patipong, Tanutcha, Hibino, Takashi, Kageyama, Hakuto, Waditee-Sirisattha, Rungaroon
• Format: Journal Article
• Language: English
• Published: Tokyo Springer Japan 01-05-2020; Springer Nature B.V
• Subjects: Adaptation; Bacterial Proteins; Biochemistry; Biomedical and Life Sciences; Biotechnology; Casein; Cyanobacteria; Degradation; Denaturation; Gene expression; Heat stress; Heat tolerance; High temperature; Homeostasis; HtrA protein; Life Sciences; Localization; Lysozyme; Membranes; Microbial Ecology; Microbiology; Original Paper; Protein biosynthesis; Protein denaturation; Protein synthesis; Proteins; Proteolysis; Proteostasis; Recombinant Proteins; Recombinants; Salinity tolerance; Salts; Serine; Serine Endopeptidases; Serine proteinase; Space life sciences; Substrates; Survival; Serine protease; HtrA; Salt stress; Halotolerant cyanobacterium; Halothece
• ISSN: 1431-0651; 1433-4909
• DOI: 10.1007/s00792-020-01162-4

The HtrA protein family represents an important class of serine proteases that are widely distributed across taxa. These evolutionarily conserved proteins are crucial for survival and function as monitors of protein synthesis during various stresses. Here, we performed gene expression analysis of the entire set of putative serine protease genes in
Halothece
sp. PCC7418 under salt stress conditions. The gene-encoding HtrA2 (
H3553
) was highly upregulated. This gene was cloned and functionally characterized, and its sub-cellular localization was determined. The recombinant H3553 protein (rH3553) displayed a pH optimum of 8.0, remained stable at 45 °C, and its proteolytic activity was not affected by salts. H3553 completely degraded the unfolded model protein, β-casein. In contrast, the folded model substrates (lysozyme or BSA) were not degraded by rH3553. Denaturation of BSA at a high temperature significantly increased its degradation by rH3553. H3553 was detected in the soluble protein fraction as well as the plasma membrane and thylakoid membrane fractions. Interestingly, the majority of H3553 was present in the plasma membrane under salt and heat stress conditions. Thus, H3553 resides in multiple sub-cellular locations and its localization drastically changes after exposure to stresses. Taken together, H3553 underpins protein quality-control process and is involved in the response and adaptation to salinity and heat stresses.