ArticleThe Biochemical journal2011
Recombinant Deg/HtrA proteases from Synechocystis sp. PCC 6803 differ in substrate specificity, biochemical characteristics and mechanism.
Article in The Biochemical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- Heterologous Expression, Purification, and Characterization of a High-Temperature Requirement A (HtrA) Protease Homologue from Leptospira.Applied biochemistry and biotechnology · 2025Article
- Diurnal rhythm causes metabolic crises in the cyanobacterial mutants of c-di-AMP signaling cascade.iScience · 2025Article
- Purification and Characterization of a DegP-Type Protease from the Marine BacteriumMicroorganisms · 2023Article
- Insights into the phylogeny and transcriptional response of serine proteases in a halotolerant cyanobacteriumPlant signaling & behavior · 2021Article
- Absence of KpsM (Slr0977) Impairs the Secretion of Extracellular Polymeric Substances (EPS) and Impacts Carbon Fluxes inmSphere · 2021Article
- Functional analysis and cryo-electron microscopy ofGut microbes · 2020Article
- The evolutionarily conserved HtrA is associated with stress tolerance and protein homeostasis in the halotolerant cyanobacterium Halothece sp. PCC7418.Extremophiles : life under extreme conditions · 2020Article
- Properties of the HtrA Protease From BacteriumFrontiers in microbiology · 2019Article
- Release of an HtrA-Like Protease from the Cell Surface of ThermophilicFrontiers in microbiology · 2017Article
- HtrA Is Important for Stress Resistance and Virulence in Haemophilus parasuis.Infection and immunity · 2016Article
- Calcium binding protects E-cadherin from cleavage by Helicobacter pylori HtrA.Gut pathogens · 2016Article
- Insights into the Cyanobacterial Deg/HtrA Proteases.Frontiers in plant science · 2016Article
- Using the SUBcellular database for Arabidopsis proteins to localize the Deg protease family.Frontiers in plant science · 2014Article
- The stability and activity of recombinant Helicobacter pylori HtrA under stress conditions.Journal of basic microbiology · 2013Article
- The HtrA protease from Streptococcus pneumoniae digests both denatured proteins and the competence-stimulating peptide.The Journal of biological chemistry · 2012Article
- Crystal structure of the yeast metacaspase Yca1.The Journal of biological chemistry · 2012Article
- The family of Deg/HtrA proteases in plants.BMC plant biology · 2012Article
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Authors and funding
7 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cyanobacteria require efficient protein-quality-control mechanisms to survive under dynamic, often stressful, environmental conditions. It was reported that three serine proteases, HtrA (high temperature requirement A), HhoA (HtrA homologue A) and HhoB (HtrA homologue B), are important for survival of Synechocystis sp. PCC 6803 under high light and temperature stresses and might have redundant physiological functions. In the present paper, we show that all three proteases can degrade unfolded model substrates, but differ with respect to cleavage sites, temperature and pH optima. For recombinant HhoA, and to a lesser extent for HtrA, we observed an interesting shift in the pH optimum from slightly acidic to alkaline in the presence of Mg2+ and Ca2+ ions. All three proteases formed different homo-oligomeric complexes with and without substrate, implying mechanistic differences in comparison with each other and with the well-studied Escherichia coli orthologues DegP (degradation of periplasmic proteins P) and DegS. Deletion of the PDZ domain decreased, but did not abolish, the proteolytic activity of all three proteases, and prevented substrate-induced formation of complexes higher than trimers by HtrA and HhoA. In summary, biochemical characterization of HtrA, HhoA and HhoB lays the foundation for a better understanding of their overlapping, but not completely redundant, stress-resistance functions in Synechocystis sp. PCC 6803.
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