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Characterizing interactions of ER resident proteins in situ through the YST-PPI method
  • +7
  • Xian Fan,
  • Huahua He,
  • Ting Wang,
  • Pan Xu,
  • Faying Zhang,
  • Shantong Hu,
  • Yueli Yun,
  • Meng Mei,
  • Guimin Zhang,
  • Li Yi
Xian Fan
Hubei University
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Huahua He
Hubei University
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Ting Wang
Hubei University
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Pan Xu
Hubei University
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Faying Zhang
Hubei University
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Shantong Hu
Beijing University of Chemical Technology
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Yueli Yun
Hubei University
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Meng Mei
Hubei University
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Guimin Zhang
Beijing University of Chemical Technology
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Li Yi
Hubei University

Corresponding Author:liyi@hubu.edu.cn

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Abstract

The mutual interactions of ER resident proteins in the ER maintain its functions, prompting the protein folding, modification, and transportation. Here, a new method, named YST-PPI (YESS-based Split fast TEV protease System for Protein-protein Interaction) was developed, targeting the characterization of protein interactions in ER. YST-PPI method integrated the YESS system, split-TEV technology and endoplasmic reticulum retention signal peptide (ERS) to provide an effective strategy for studying ER in situ PPIs in a fast and quantitative manner. The interactions among 15 ER resident proteins of S. cerevisiae were explored using the YST-PPI system, and their interaction network map was constructed, in which more than 74 interacting resident protein pairs were identified. Our studies also showed that Lhs1p plays a critical role in regulating the interactions of most of the ER resident proteins, expect the Sil1p, indicating its potential role in controlling the ER molecular chaperones. Moreover, the mutual interaction revealed by our studies further confirmed that the ER resident proteins perform their functions in a synergetic way and multimer complex might be formed during the process.
Submitted to Biotechnology Journal
27 May 2024Assigned to Editor
27 May 2024Submission Checks Completed
29 May 2024Reviewer(s) Assigned
22 Jun 2024Review(s) Completed, Editorial Evaluation Pending
01 Aug 20241st Revision Received
02 Aug 2024Submission Checks Completed
02 Aug 2024Assigned to Editor
02 Aug 2024Review(s) Completed, Editorial Evaluation Pending
02 Aug 2024Reviewer(s) Assigned
09 Aug 2024Editorial Decision: Revise Minor
14 Aug 20242nd Revision Received
14 Aug 2024Submission Checks Completed
14 Aug 2024Assigned to Editor
14 Aug 2024Review(s) Completed, Editorial Evaluation Pending
16 Aug 2024Editorial Decision: Accept