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

Autor:	Yui Satake, Makoto Hirano, Kiichiro Totani, Kaoru Arima, Taiki Kuribara
Rok vydání:	2020
Předmět:	Chemistry genetic structures biology General Chemical Engineering Endoplasmic reticulum biology.protein General Chemistry Binding immunoglobulin protein QD1-999 Calreticulin Article Cell biology
Zdroj:	ACS Omega, Vol 5, Iss 13, Pp 7399-7405 (2020) ACS Omega
ISSN:	2470-1343
DOI:	10.1021/acsomega.9b04445
Popis:	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. In the absence of ATP, GRP94 and CRT preferentially recognized misfolded myoglobin (α-helix-rich protein), whereas BiP preferentially recognized misfolded RNase A (α-helix/β-sheet mixed protein) and β-lactoglobulin (β-sheet-rich protein). The preferential order of ER chaperones may be dynamically regulated by ER conditions and the higher-order structure of client proteins.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7da5107fdbf3fbfcfe2b0ea7e80c55a7 https://doi.org/10.1021/acsomega.9b04445 Zobrazit plný text záznamu