ArticleBMC evolutionary biology2010
Evolution and thermodynamics of the slow unfolding of hyperstable monomeric proteins.
Article in BMC evolutionary biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 32 citations in OpenAlex.
- Three Molecular Modification Strategies to Improve the Thermostability of Xylanase XynA fromFoods (Basel, Switzerland) · 2023Article
- Design of a Protein with Improved Thermal Stability by an Evolution-Based Generative Model.Angewandte Chemie (International ed. in English) · 2022Article
- Evolution of Protein Structure and Stability in Global Warming.International journal of molecular sciences · 2020Review
- Thermophilic Proteins as Versatile Scaffolds for Protein Engineering.Microorganisms · 2018Review
- Protein Evolution is Potentially Governed by Protein Stability: Directed Evolution of an Esterase from the Hyperthermophilic Archaeon Sulfolobus tokodaii.Journal of molecular evolution · 2018Article
- Multifactorial level of extremostability of proteins: can they be exploited for protein engineering?Extremophiles : life under extreme conditions · 2017Review
- Characterization of two key enzymes for aromatic amino acid biosynthesis in symbiotic archaea.Extremophiles : life under extreme conditions · 2016Article
- Psychrophilic enzymes: from folding to function and biotechnology.Scientifica · 2013Review
- Stabilization by fusion to the C-terminus of hyperthermophile Sulfolobus tokodaii RNase HI: a possibility of protein stabilization tag.PloS one · 2011Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe unfolding speed of some hyperthermophilic proteins is dramatically lower than that of their mesostable homologs. Ribonuclease HII from the hyperthermophilic archaeon Thermococcus kodakaraensis (Tk-RNase HII) is stabilized by its remarkably slow unfolding rate, whereas RNase HI from the thermophilic bacterium Thermus thermophilus (Tt-RNase HI) unfolds rapidly, comparable with to that of RNase HI from Escherichia coli (Ec-RNase HI).
resultsTo clarify whether the difference in the unfolding rate is due to differences in the types of RNase H or differences in proteins from archaea and bacteria, we examined the equilibrium stability and unfolding reaction of RNases HII from the hyperthermophilic bacteria Thermotoga maritima (Tm-RNase HII) and Aquifex aeolicus (Aa-RNase HII) and RNase HI from the hyperthermophilic archaeon Sulfolobus tokodaii (Sto-RNase HI). These proteins from hyperthermophiles are more stable than Ec-RNase HI over all the temperature ranges examined. The observed unfolding speeds of all hyperstable proteins at the different denaturant concentrations studied are much lower than those of Ec-RNase HI, which is in accordance with the familiar slow unfolding of hyperstable proteins. However, the unfolding rate constants of these RNases H in water are dispersed, and the unfolding rate constant of thermophilic archaeal proteins is lower than that of thermophilic bacterial proteins.
conclusionsThese results suggest that the nature of slow unfolding of thermophilic proteins is determined by the evolutionary history of the organisms involved. The unfolding rate constants in water are related to the amount of buried hydrophobic residues in the tertiary structure.
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