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Perturbation of the Relative Contribution of Molecular Chaperones in the Endoplasmic Reticulum.


ABSTRACT: We demonstrate the preferential orders of molecular chaperones glucose-regulated protein 94 (GRP94), binding immunoglobulin protein (BiP), and calreticulin (CRT) in an endoplasmic reticulum (ER) fraction from rat liver using columns conjugated with denatured myoglobin, RNase A, or ?-lactoglobulin as client proteins in the presence or absence of ATP. The results showed that BiP, CRT, and GRP94 preferentially contributed myoglobin, RNase A, and ?-lactoglobulin, respectively, in the presence of ATP. In the absence of ATP, GRP94 and CRT preferentially recognized misfolded myoglobin (?-helix-rich protein), whereas BiP preferentially recognized misfolded RNase A (?-helix/?-sheet mixed protein) and ?-lactoglobulin (?-sheet-rich protein). The preferential order of ER chaperones may be dynamically regulated by ER conditions and the higher-order structure of client proteins.

SUBMITTER: Totani K 

PROVIDER: S-EPMC7144178 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature

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Perturbation of the Relative Contribution of Molecular Chaperones in the Endoplasmic Reticulum.

Totani Kiichiro K   Arima Kaoru K   Kuribara Taiki T   Satake Yui Y   Hirano Makoto M  

ACS omega 20200324 13


We demonstrate the preferential orders of molecular chaperones glucose-regulated protein 94 (GRP94), binding immunoglobulin protein (BiP), and calreticulin (CRT) in an endoplasmic reticulum (ER) fraction from rat liver using columns conjugated with denatured myoglobin, RNase A, or β-lactoglobulin as client proteins in the presence or absence of ATP. The results showed that BiP, CRT, and GRP94 preferentially contributed myoglobin, RNase A, and β-lactoglobulin, respectively, in the presence of ATP  ...[more]

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