An improved method for the heterologous production of soluble human ribosomal proteins in Escherichia coli

Danilo Correddu, José de Jesús Montaño López, Praveen G. Vadakkedath, Amy Lai, Jane I. Pernes, Paris R. Watson, Ivanhoe K.H. Leung*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

9 Citations (Scopus)
218 Downloads (Pure)


Human ribosomal proteins play important structural and functional roles in the ribosome and in protein synthesis. An efficient method to recombinantly produce and purify these proteins would enable their full characterisation. However, the production of human ribosomal proteins can be challenging. The only published method about the recombinant production of human ribosomal proteins involved the recovery of proteins from inclusion bodies, a process that is tedious and may lead to significant loss of yield. Herein, we explored the use of different Escherichia coli competent cells and fusion protein tags for the recombinant production of human ribosomal proteins. We found that, by using thioredoxin as a fusion protein, soluble ribosomal protein could be obtained directly from cell lysates, thus leading to an improved method to recombinantly produce these proteins.

Original languageEnglish
Article number8884
Number of pages8
JournalScientific Reports
Issue number1
Publication statusPublished - 20 Jun 2019

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