Alpha-crystallin: an ATP-independent complete molecular chaperone toward sorbitol dehydrogenase

Marini, I; Moschini, Roberta; Corso, Antonella Del; Mura, Umberto

doi:10.1007/s00018-005-4474-z

Cited by 12 publications

(14 citation statements)

References 123 publications

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“…Similarly to what has been previously reported for a-crystallin [33], thermal inactivation of SDH is prevented by BSA. This is shown in fi gure 1, where the effectiveness of BSA and a-crystallin in protecting the functional integrity of the enzyme are compared.…”

Section: Prevention Of Thermally Induced Inactivation Of Enzymes By Bsasupporting

confidence: 70%

“…As postulated for the effect of ATP on the a-crystallin-assisted SDH refolding [34], the possibility that ATP or ADP may interact with the target protein, mimicking the enzyme co-factor NADH, cannot be ruled out. Calcium ion, which like Mg 2+ [44] was previously shown to impair the protective action of a-crystallin towards thermally induced aggregation of ALR2 [45], as well as inactivation and aggregation of SDH [33], also exerts its effect on the protective action of BSA on thermally stressed SDH. As previously observed for a-crystallin [33,45], Ca 2+ , in the concentration range of 0.1-0.5 mM, at 55 °C and at a protector:SDH ratio of 1:1, is able to abolish the protective action of BSA towards the thermally stressed enzyme (data not shown).…”

Section: Discussionmentioning

confidence: 96%

“…Calcium ion, which like Mg 2+ [44] was previously shown to impair the protective action of a-crystallin towards thermally induced aggregation of ALR2 [45], as well as inactivation and aggregation of SDH [33], also exerts its effect on the protective action of BSA on thermally stressed SDH. As previously observed for a-crystallin [33,45], Ca 2+ , in the concentration range of 0.1-0.5 mM, at 55 °C and at a protector:SDH ratio of 1:1, is able to abolish the protective action of BSA towards the thermally stressed enzyme (data not shown). The only chaperone feature for which the effectiveness of BSA is rather poor with respect to a-crystallin is the antiaggregation ability towards thermally stressed proteins.…”

Section: Discussionmentioning

confidence: 96%

“…Worth noting here is the previous observation that the protective action of a-crystallin towards aggregation and inactivation of thermally stressed SDH was shown to occur through the formation of two kinds of interacting adducts: the fi rst, stable and containing inactive SDH, possibly related to the antiaggregation action of a-crystallin; the second, transient and containing active SDH, appears to be related to the preservation of SDH activity. The fi rst complex has a high molecular weight, suggesting interaction between multimeric 800 kDa a-crystallin with the target protein; the second has a weight comparable to that of SDH, suggesting interaction between enzyme and oligomeric a-crystallin complexes [33]. BSA, which is uncapable of extensive multimeric assembly and has a surface hydrophobicity reduced rather than expanded by a temperature increase [23], may only be able to afford interaction sites for the second type of complex.…”

Section: Discussionmentioning

confidence: 99%

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Chaperone-like features of bovine serum albumin: a comparison with α-crystallin

Marini

Moschini

Corso

et al. 2005

Cell. Mol. Life Sci.

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The chaperone behaviour of bovine serum albumin was compared with that of alpha-crystallin. The chaperone activity was assessed by measuring: (i) the ability to antagonize protein aggregation induced by heat; (ii) the capability to protect the activity of thermally stressed enzymes and (iii) the effectiveness in assisting the functional recovery of chemically denatured sorbitol dehydrogenase. Despite the lack of structural analogies, both proteins show several functional similarities in preventing inactivation of thermally stressed enzymes and in reactivating chemically denatured sorbitol dehydrogenase. As with alpha-crystallin, the chaperone action of bovine serum albumin appears to be ATP independent. Bovine serum albumin appears significantly less effective than alpha-crystallin only in preventing thermally induced protein aggregation. A possible relationship between chaperone function and structural organization is proposed. Together, our results indicate that bovine serum albumin acts as a molecular chaperone and that, for its particular distribution, can be included in the extracellular chaperone family.

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Section: Prevention Of Thermally Induced Inactivation Of Enzymes By Bsasupporting

confidence: 70%

Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

Chaperone-like features of bovine serum albumin: a comparison with α-crystallin

Marini

Moschini

Corso

et al. 2005

Cell. Mol. Life Sci.

Self Cite

View full text Add to dashboard Cite

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“…Though the enzyme activity was regained~3% higher in presence of ATP-associated α-crystallin than α-crystallin only, but ATP did not show much significant effect on the refolding yield of Table 2). This type of observation was found in case of sorbitol dehydrogenase [26].…”

Section: Effect Of Adenine Nucleotides On α-Crystallin-mediated Renatmentioning

confidence: 80%

In Vitro Renaturation of Alkaline Family G/11 Xylanase via a Folding Intermediate: α-Crystallin Facilitates Refolding in an ATP-Independent Manner

Dutta

Bhattacharjee

Majumdar

et al. 2009

Appl Biochem Biotechnol

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In this study, alkaliphilic family G/11 xylanase from alkali-tolerant filamentous fungi Penicillium citrinum MTCC 6489 was used as a model system to gain insight into the molecular aspects of unfolding/refolding of alkaliphilic glycosyl hydrolase protein family. The intrinsic protein fluorescence suggested a putative intermediate state of protein in presence of 2 M guanidium hydrochloride (GdmCl) with an emission maximum of 353 nm. Here we studied the refolding of GdmCl-denatured alkaline xylanase in the presence and the absence of a multimeric chaperone protein alpha-crystallin to elucidate the molecular mechanism of intramolecular interactions of the alkaliphilic xylanase protein that dictates its extremophilic character. Our results, based on intrinsic tryptophan fluorescence and hydrophobic fluorophore 8-anilino-1- naphthalene sulfonate-binding studies, suggest that alpha-crystallin formed a complex with a putative molten globule-like intermediate in the refolding pathway of xylanase in an ATP-independent manner. A 2 M GdmCl is sufficient to denature alkaline xylanase completely. The hydrodynamic radius (R(H)) of a native alkaline xylanase is 4.0, which becomes 5.0 in the presence of 2 M GdmCl whereas in presence of the higher concentration of GdmCl R(H) value was shifted to 100, indicating the aggregation of denatured xylanase. The alpha-crystallin.xylanase complex exhibited the recovery of functional activity with the extent of approximately 43%. Addition of ATP to the complex did not show any significant effect on activity recovery of the denatured protein.

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Structure, function, property, and role in neurologic diseases and other diseases of the sHsp22

Chen

Zhang

et al. 2007

J of Neuroscience Research

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Small heat shock proteins are members of the heat shock proteins family. They share important identical features: 1) they form the conserved structure 'alpha-crystallin domain' with about 80-100 residues in the C-terminal part of the proteins; 2) they have monomeric molecular masses ranging in 12-43 kDa; 3) they associate into large oligomers consisting in many cases of subunits; 4) they increase expression under stress conditions; 5) they exhibit a highly dynamic structure; and 6) they play a chaperone-like role. Hsp22 (also known as HspB8, H11, and E2IG1) retains the structural motif of the 'alpha-crystallin' family of Hsps and is a member of the superfamily of sHsps. Hsp22 displays chaperone activity, autokinase activity, and trigger or block apoptosis activity. It differs from canonical family members existing as a monomer. A decrease in the HspB8 activity may contribute to the development of some neurologic diseases and others.

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Alpha-crystallin: an ATP-independent complete molecular chaperone toward sorbitol dehydrogenase

Cited by 12 publications

References 123 publications

Chaperone-like features of bovine serum albumin: a comparison with α-crystallin

Chaperone-like features of bovine serum albumin: a comparison with α-crystallin

In Vitro Renaturation of Alkaline Family G/11 Xylanase via a Folding Intermediate: α-Crystallin Facilitates Refolding in an ATP-Independent Manner

Structure, function, property, and role in neurologic diseases and other diseases of the sHsp22

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