期刊
PROTEIN EXPRESSION AND PURIFICATION
卷 193, 期 -, 页码 -出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pep.2022.106061
关键词
Leucine-rich repeats; SHOC2; Chaperones; Protein complexes; Structural biology; Baculovirus
类别
资金
- National Institutes of Health [75N91019D00024]
This study demonstrates that the co-expression of SUGT1 chaperone with polycistronic protein expression in baculovirus-infected insect cells can greatly enhance the production yield and quality of recombinant proteins.
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 leucinerich repeat proteins.
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