Please use this identifier to cite or link to this item: doi:10.22028/D291-36750
Title: How does Sec63 affect the conformation of Sec61 in yeast?
Author(s): Bhadra, Pratiti
Yadhanapudi, Lalitha
Römisch, Karin
Helms, Volkhard
Language: English
Title: PLoS Computational Biology
Volume: 17
Issue: 3
Publisher/Platform: Plos
Year of Publication: 2021
DDC notations: 500 Science
Publikation type: Journal Article
Abstract: The Sec complex catalyzes the translocation of proteins of the secretory pathway into the endoplasmic reticulum and the integration of membrane proteins into the endoplasmic reticulum membrane. Some substrate peptides require the presence and involvement of accessory proteins such as Sec63. Recently, a structure of the Sec complex from Saccharomyces cerevisiae, consisting of the Sec61 channel and the Sec62, Sec63, Sec71 and Sec72 proteins was determined by cryo-electron microscopy (cryo-EM). Here, we show by co-precipitation that the Sec61 channel subunit Sbh1 is not required for formation of stable Sec63-Sec61 contacts. Molecular dynamics simulations started from the cryo-EM conformation of Sec61 bound to Sec63 and of unbound Sec61 revealed how Sec63 affects the conformation of Sec61 lateral gate, plug, pore region and pore ring diameter via three intermolecular contact regions. Molecular docking of SRP-dependent vs. SRP-independent signal peptide chains into the Sec61 channel showed that the pore regions affected by presence/absence of Sec63 play a crucial role in positioning the signal anchors of SRP-depen dent substrates nearby the lateral gate.
DOI of the first publication: 10.1371/journal.pcbi.1008855
URL of the first publication:
Link to this record: urn:nbn:de:bsz:291--ds-367501
ISSN: 1553-7358
Date of registration: 11-Jul-2022
Description of the related object: Supporting information
Related object:
Faculty: NT - Naturwissenschaftlich- Technische Fakultät
Department: NT - Biowissenschaften
Professorship: NT - Prof. Dr. Volkhard Helms
NT - Prof. Dr. Karin Römisch
Collections:SciDok - Der Wissenschaftsserver der Universität des Saarlandes

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