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Polycistronic baculovirus expression of SUGT1 enables high-yield production of recombinant leucine-rich repeat proteins and protein complexes

  1. Author:
    Snead,Kelly
    Wall,Vanessa
    Ambrose,Hannah
    Esposito,Dom
    Drew,Matt

  2. Author Address

    Protein Expression Laboratory, NCI RAS Initiative, Cancer Research Technology Program, Frederick National Laboratory for Cancer Research, Frederick, MD, USA., Protein Expression Laboratory, NCI RAS Initiative, Cancer Research Technology Program, Frederick National Laboratory for Cancer Research, Frederick, MD, USA. Electronic address: matt.drew@nih.gov.,
    1. Year: 2022
    2. Date: Feb 04
    3. Epub Date: 2022 02 04
  2. Journal: Protein Expression and Purification
  3. Elsevier Science
    1. 193
    2. Pages: 106061
  5. Type of Article: Article
  6. Article Number: 106061
  1. Abstract:

    The SHOC2-MRAS-PPP1CA (SMP) complex is a holoenzyme that plays a vital role in the MAP kinase signaling pathway. Previous attempts to produce this challenging three-protein complex have relied on co-infection with multiple viruses and the use of affinity tags to attempt to isolate functional recombinant protein complexes. Leucine-rich repeat containing proteins have been historically challenging to express, and we hypothesized that co-expression of appropriate chaperones may be necessary for optimal production. We describe here how the SUGT1 chaperone can, in conjunction with polycistronic protein expression in baculovirus-infected insect cells, dramatically enhance production yield and quality of recombinant SHOC2, the SMP complex, and other leucine-rich repeat proteins. Copyright © 2022. Published by Elsevier Inc.

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External Sources

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  2. DOI: 10.1016/j.pep.2022.106061
  3. PMID: 35131438
  4. PII : S1046-5928(22)00018-3

Library Notes

  1. Fiscal Year: FY2021-2022
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