Co-expression of human chaperone Hsp70 and Hsdj or Hsp40 co-factor increases solubility of overexpressed target proteins in insect cells

Naoaki Yokoyama, Mineo Hirata, Kenzo Ohtsuka, Yukihiro Nishiyama, Ken Fujii, Masatoshi Fujita, Kiyotaka Kuzushima, Tohru Kiyono, Tatsuya Tsurumi

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

The insect-baculovirus expression system has proved particularly useful for producing recombinant proteins that are biologically active. Overexpression of foreign proteins using the recombinant baculovirus system is often accompanied by aggregation of the overexpressed protein, which is thought to be due to a limitation of the translated protein folding in the infected cells. Co-infection of a recombinant baculovirus capable of expressing the human chaperone Hsp70 slightly increased the solubility of the overexpressed Epstein-Barr virus replication protein, BZLF1. Co-expression of Hsp70 and its co-factor, Hsdj or Hsp40, was here found to improve the solubility of the target protein several fold. Thus, a baculovirus expression system producing these molecular chaperones may find application for improved production of target foreign gene products in insect cells. (C) 2000 Elsevier Science B.V.

Original languageEnglish
Pages (from-to)119-124
Number of pages6
JournalBiochimica et Biophysica Acta - Gene Structure and Expression
Volume1493
Issue number1-2
DOIs
Publication statusPublished - Sep 7 2000
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Genetics

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