Background: Secretory proteins acquire their native three-dimensional conformation through repeated brief interactions with ER chaperones and oxidoreductases. Results: We have captured and defined previously-unidentified disulfide adducts of newly-synthesized thyroglobulin with ERp72 and CaBP1/P5. Conclusion: Multiple oxidoreductases simultaneously engage thyroglobulin during its early folding in the ER. Significance: Distinct chaperone/oxidoreductase partners coordinately engage this multi-domain secretory protein to promote its advancement to the native state.

Transient Covalent Interactions of Newly-Synthesized Thyroglobulin with Oxidoreductases of the Endoplasmic Reticulum

DI JESO, Bruno
Primo
Membro del Collaboration Group
;
TREGLIA, Antonella Sonia;LOFRUMENTO, Dario Domenico
Membro del Collaboration Group
;
NICOLARDI, Giuseppe;
2014-01-01

Abstract

Background: Secretory proteins acquire their native three-dimensional conformation through repeated brief interactions with ER chaperones and oxidoreductases. Results: We have captured and defined previously-unidentified disulfide adducts of newly-synthesized thyroglobulin with ERp72 and CaBP1/P5. Conclusion: Multiple oxidoreductases simultaneously engage thyroglobulin during its early folding in the ER. Significance: Distinct chaperone/oxidoreductase partners coordinately engage this multi-domain secretory protein to promote its advancement to the native state.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11587/384033
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