ArticleProtein science : a publication of the Protein Society2005
pH effects on the stability and dimerization of procaspase-3.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Sequential Unfolding Mechanisms of Monomeric Caspases.Biochemistry · 2023Article
- Sequential unfolding mechanisms of monomeric caspases.bioRxiv : the preprint server for biology · 2023Article
- Comparing the folding landscapes of evolutionarily divergent procaspase-3.Bioscience reports · 2022Article
- Evolution of the folding landscape of effector caspases.The Journal of biological chemistry · 2021Article
- Modifications to a common phosphorylation network provide individualized control in caspases.The Journal of biological chemistry · 2018Article
- Substrate and inhibitor-induced dimerization and cooperativity in caspase-1 but not caspase-3.The Journal of biological chemistry · 2013Article
- Monomeric banana lectin at acidic pH overrules conformational stability of its native dimeric form.PloS one · 2013Article
- Death by caspase dimerization.Advances in experimental medicine and biology · 2012Review
- Design and characterization of an enhanced repressor of human papillomavirus E2 protein.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011Article
- Thermodynamic, enzymatic and structural effects of removing a salt bridge at the base of loop 4 in (pro)caspase-3.Archives of biochemistry and biophysics · 2011Article
- Melody, an ENU mutation in Caspase 3, alters the catalytic cysteine residue and causes sensorineural hearing loss in mice.Mammalian genome : official journal of the International Mammalian Genome Society · 2010Article
- Folding and assembly kinetics of procaspase-3.Protein science : a publication of the Protein Society · 2009Article
- Role of loop bundle hydrogen bonds in the maturation and activity of (Pro)caspase-3.Biochemistry · 2006Article
- Reassembly of active caspase-3 is facilitated by the propeptide.The Journal of biological chemistry · 2005Article
- Oligomerization endows enormous stability to soybean agglutinin: a comparison of the stability of monomer and tetramer of soybean agglutinin.Biophysical journal · 2005Article
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2 authors.
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Abstract
pH-dependent conformational changes are known to occur in dimeric procaspase-3, and they have been shown to affect the rate of automaturation. We studied the equilibrium unfolding of procaspase-3(C163S) as a function of pH (between pH 8.5 and pH 4) in order to examine these changes in the context of folding and stability. The data show that the procaspase dimer undergoes a pH-dependent dissociation below pH 5, so that the protein is mostly monomeric at pH 4. Consistent with this, the dimer unfolds via a four-state process between pH 8.5 and pH 4.75, in which the native dimer isomerizes to a dimeric intermediate, and the dimeric intermediate dissociates to a monomer, which then unfolds. In contrast, a small protein concentration dependence was observed by circular dichroism, but not by fluorescence emission, at pH 4.5 and pH 4.2. There was no protein-concentration dependence to the data collected at pH 4. Overall, the results are consistent with the redistribution of the population of native dimer (N(2)) to dimeric intermediate (I(2)) to monomeric intermediate (I), as the pH is lowered so that at pH 4, the "native" ensemble resembles the monomeric intermediate (I) observed during unfolding at higher pH. An emerging picture of the monomeric procaspase is discussed. Procaspase-3 is most stable at pH approximately 7 (24-26 kcal/mol), and while the stability decreased with pH, it was observed that dimerization contributes the majority (>70%) of the conformational free energy.
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