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Binding of ?-crystallin substrate prevents the binding of copper and zinc ions to the molecular chaperone ?-crystallin.

ABSTRACT: ?-Crystallin is a small heat shock protein and molecular chaperone. Binding of Cu2+ and Zn2+ ions to ?-crystallin leads to enhanced chaperone function. Sequestration of Cu2+ by ?-crystallin prevents metal-ion mediated oxidation. Here we show that binding of human ?D-crystallin (HGD, a natural substrate) to human ?A-crystallin (HAA) is inversely related to the binding of Cu2+/Zn2+ ions: The higher the amount of bound HGD, the lower the amount of bound metal ions. Thus, in the aging lens, depletion of free HAA will not only lower chaperone capacity but also lower Cu2+ sequestration, thereby promoting oxidation and cataract.

SUBMITTER: Ghosh KS

PROVIDER: S-EPMC3081693 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature

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Binding of γ-crystallin substrate prevents the binding of copper and zinc ions to the molecular chaperone α-crystallin.

Ghosh Kalyan S KS Pande Ajay A Pande Jayanti J

Biochemistry 20110330 16

α-Crystallin is a small heat shock protein and molecular chaperone. Binding of Cu2+ and Zn2+ ions to α-crystallin leads to enhanced chaperone function. Sequestration of Cu2+ by α-crystallin prevents metal-ion mediated oxidation. Here we show that binding of human γD-crystallin (HGD, a natural substrate) to human αA-crystallin (HAA) is inversely related to the binding of Cu2+/Zn2+ ions: The higher the amount of bound HGD, the lower the amount of bound metal ions. Thus, in the aging lens, depletio ...[more]

PMID: 21417258

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Project description:BiP overexpression improves leaf water relations during droughts and delays drought-induced leaf senescence. However, whether BiP controls cellular homeostasis under drought conditions or simply delays dehydration-induced leaf senescence as the primary cause for water stress tolerance remains to be determined. To address this issue, we examined the drought-induced transcriptomes of BiP-overexpressing lines and wild-type (WT) lines under similar leaf water potential (?w) values. In the WT leaves, a ?w reduction of -1.0 resulted in 1339 up-regulated and 2710 down-regulated genes; in the BiP-overexpressing line 35S::BiP-4, only 334 and 420 genes were induced and repressed, respectively, at a similar leaf ?w?=?-1.0 MPa. This level of leaf dehydration was low enough to induce a repertory of typical drought-responsive genes in WT leaves but not in 35S::BiP-4 dehydrated leaves. The responders included hormone-related genes, functional and regulatory genes involved in drought protection and senescence-associated genes. The number of differentially expressed genes in the 35S::BiP-4 line approached the wild type number at a leaf ?w?=?-1.6 MPa. However, N-rich protein (NRP)- mediated cell death signaling genes and unfolded protein response (UPR) genes were induced to a much lower extent in the 35S::BiP-4 line than in the WT even at ?w?=?-1.6 MPa. The heatmaps for UPR, ERAD (ER-associated degradation protein system), drought-responsive and cell death-associated genes revealed that the leaf transcriptome of 35S::BiP-4 at ?w?=?-1.0 MPa clustered together with the transcriptome of well-watered leaves and they diverged considerably from the drought-induced transcriptome of the WT (?w?=?-1.0, -1.7 and -2.0 MPa) and 35S::BiP-4 leaves at ?w?=?-1.6 MPa. Taken together, our data revealed that BiP-overexpressing lines requires a much higher level of stress (?w?=?-1.6 MPa) to respond to drought than that of WT (?w?=?-1.0). Therefore, BiP overexpression maintains cellular homeostasis under water stress conditions and thus ameliorates endogenous osmotic stress.

Dataset Information

Binding of ?-crystallin substrate prevents the binding of copper and zinc ions to the molecular chaperone ?-crystallin.

Publications

Binding of γ-crystallin substrate prevents the binding of copper and zinc ions to the molecular chaperone α-crystallin.

Similar Datasets

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