pH-Induced Reversible Dissociation of Tetrameric Duck Lens Delta-Crystallin

Chang, Gu‐Gang; Lee, Hwei-Jen; Chow, Rue-Huan

doi:10.1006/exer.1997.0372

Cited by 8 publications

(10 citation statements)

References 23 publications

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“…Our previous results indicated that δ2‐crystallin underwent tetramer/dimer/monomer dissociation–reassociation interconversion under acidic conditions [17]. These results are in accordance with the crystal structure of δ‐crystallin in that subunits A and B form a closely interacting dimer.…”

Section: Discussionsupporting

confidence: 87%

“…Relative molecular mass of d2-crystallin in GdnHCl solution d-Crystallin is a tetrameric protein with a double dimeric structure [11,13,17]. The biphasic transition curve of protein molecular ellipticity and fluorescence as a function of GdnHCl concentration might suggest the involvement of a dissociation process (Fig.…”

Section: Guanidine Hydrochloride Induced Denaturation-renaturation Ofmentioning

confidence: 99%

“…The previous reports by Piatigorsky and colleagues demonstrated that embryonic chicken δ‐crystallin contained a high helix content and was not completely dissociated by treatment with high concentration of urea or guanidinium hydrochloride (GdnHCl) [15,16]. Duck δ‐crystallin apparently dissociated into dimers and monomers under acidic conditions [17]. Recently, under the effect of GdnHCl the recombinant duck δ2 crystallin and human argininosuccinate lyase were shown to have biphasic dissociation/denaturation protein structural changes when monitored by CD [18,19].…”

mentioning

confidence: 99%

“…The previous reports by Piatigorsky and colleagues demonstrated that embryonic chicken d-crystallin contained a high helix content and was not completely dissociated by treatment with high concentration of urea or guanidinium hydrochloride (GdnHCl) [15,16]. Duck d-crystallin apparently dissociated into dimers and monomers under acidic conditions [17].…”

mentioning

confidence: 99%

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Guanidine hydrochloride induced reversible dissociation and denaturation of duck δ2‐crystallin

Lee

Chang

2000

European Journal of Biochemistry

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The tetrameric d2-crystallin from duck lens exhibits a reversible dissociation-denaturation process in solutions containing guanidine hydrochloride (GdnHCl). Sigmoidal or biphasic curves for the dissociation/denaturation processes, obtained using different methods of structural analysis, as a function of GdnHCl concentration were not coincidental with each other. d2-crystallin in 0.91 m GdnHCl existed primarily as a monomer, which had no endogenous argininosuccinate lyase activity. After dilution of the GdnHCl-treated protein, the monomers reassociated into tetramers with concomitant recovery of enzyme activity. The sigmoidal recovery of enzyme activity demonstrates a cooperative hysteretic reactivation process. When the concentration of GdnHCl was higher than 1.2 m, various partially unfolded soluble forms of d2-crystallin were produced from the dissociated monomers as shown by size-exclusion chromatography. The formation of a partially unfolded intermediate during the dissociation±denaturation process is proposed.Keywords: d-crystallin; lens protein; protein folding; argininosuccinate lyase; reversible dissociation/ denaturation.Crystallins, which are the most abundant soluble proteins in the vertebrate eye lens, are considered to play a structural role in maintaining a high refractory index while ensuring transparency [1±4]. Crystallins apparently evolved via gene duplication and divergence and can be classified into two groups of family members according to species distribution. The ubiquitous crystallins (a, b and g) are present in all vertebrate lenses, while the taxon-specific crystallins are found only in certain species. a-crystallins are related to the stressinducible small heat-shock proteins [5]. However, the most surprising discovery is the evolutionary strategy of gene sharing to recruit metabolic enzymes as crystallins [6]. Some of the species-specific dual functional crystallins have highly homologous sequences to these enzymes and have been found to possess enzyme activity.d-crystallin is an example of an enzyme that has been recruited as a lens protein in birds and reptiles. It accounts for about 40±70% of all the soluble proteins and in water it assembles to form a softer, more liquid-like lens with a better refractive index [7]. Two tandemly arranged genes (d1 and d2) are expressed with 88±94% protein sequence identity among the different d-crystallins and 65±71% identity to argininosuccinate lyase in the chicken and duck genomes [6]. The isolated proteins (d1 or d2) consist of four identical subunits with a molecular mass of < 200 kDa for the tetramer. Of the two forms of the enzyme, only the d2-crystallin possesses endogenous argininosuccinate lyase activity [8±10]. d-Crystallin from chicken and duck lens have similar tertiary and quaternary structures [11±14]. A 20-a-helix bundle of the tetramer comprises the predominant core of the protein, providing a putative active site cleft located at the boundary between three subunits of the tetramer (Fig. 1).The previous reports by Piatigorsky and...

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Section: Discussionsupporting

confidence: 87%

Section: Guanidine Hydrochloride Induced Denaturation-renaturation Ofmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Guanidine hydrochloride induced reversible dissociation and denaturation of duck δ2‐crystallin

Lee

Chang

2000

European Journal of Biochemistry

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“…The dimeric form of the protein was detected transiently during this process of dissociation, due to weak interactions between the two pairs in the tetramer [10]. The reversible dissociation-association process of the tetramer-dimermonomer was also pH-dependent [14]. Using the available results, the molecular mechanism for the folding of polypeptide chain and assembling of individual subunits into the native tetrameric structure was investigated.…”

Section: Introductionmentioning

confidence: 99%

The effect of N-terminal truncation on double-dimer assembly of goose δ-crystallin

Lee

Lai

et al. 2005

Biochemical Journal

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Delta-crystallin is a soluble structural protein in avian eye lenses that confers special refractive properties. In the presence of GdmCl (guanidinium chloride), tetrameric delta-crystallin undergoes dissociation via a dimeric state to a monomeric molten globule intermediate state. The latter are denatured at higher GdmCl concentrations in a multi-state manner. In the present study, the X-ray structure of goose delta-crystallin was determined to 2.8 A (1 A=0.1 nm). In this structure the first 25 N-terminal residues interact with a hydrophobic cavity in a neighbouring molecule, stabilizing the quaternary structure of this protein. When these 25 residues were deleted this did not produce any gross structural changes, as judged by CD analysis, but slightly altered tryptophan fluorescence and ANS (8-anilino-1-naphthalenesulphonic acid) spectra. The dimeric form was significantly identified as judged by sedimentation velocity and nondenaturing gradient gel electrophoresis. This mutant had increased sensitivity to temperature denaturation and GdmCl concentrations of 0.3-1.0 M. This protein was destabilized about 3.3 kcal/mol (1 kcal=4.184 kJ) due to N-terminal truncation. After incubation at 37 degrees C N-terminal truncated proteins were prone to aggregation, suggesting the presence of the unstable dimeric conformation. An important role for the N-terminus in dimer assembly of goose delta-crystallin is proposed.

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α-Crystallin protects human arginosuccinate lyase activity under freeze–thaw conditions

et al. 2012

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pH-Induced Reversible Dissociation of Tetrameric Duck Lens Delta-Crystallin

Cited by 8 publications

References 23 publications

Guanidine hydrochloride induced reversible dissociation and denaturation of duck δ2‐crystallin

Guanidine hydrochloride induced reversible dissociation and denaturation of duck δ2‐crystallin

The effect of N-terminal truncation on double-dimer assembly of goose δ-crystallin

α-Crystallin protects human arginosuccinate lyase activity under freeze–thaw conditions

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