Omics Analysis Reveals the Mechanism of Enhanced Recombinant Protein Production Under Simulated Microgravity

Jie Huangfu, Hye Su Kim, Ke Xu, Xiaoyu Ning, Lei Qin*, Jun Li, Chun Li

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

Abstract

Simulated microgravity (SMG) is regarded as a suitable environment to produce recombinant proteins. This study showed that β-glucuronidase expressing Escherichia coli had higher productivity of recombinant protein and higher plasmid copy number under SMG compared with the normal gravity condition. The cellular changes were analyzed at both transcriptomic and proteomic levels. The upregulation of a group of ribosome/RNA polymerase genes and a cluster of genes involving energy metabolism at transcriptomic level stood out for improved production of recombinant protein under SMG. The protein folding modulators such as chaperones were upregulated at proteomic level, which could be a result of the increased activity of protein synthesis and can help recombinant protein production. Protein export was also strengthened, which was revealed at both transcriptomic and proteomic levels. The results demonstrated that SMG is a favorable environment for recombinant protein production arousing the upregulation of protein synthesis, protein folding, and protein export.

Original languageEnglish
Article number30
JournalFrontiers in Bioengineering and Biotechnology
Volume8
DOIs
Publication statusPublished - 20 Feb 2020

Keywords

  • omics
  • protein folding
  • recombinant protein
  • ribosome protein assembly
  • simulated microgravity

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