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A Recombinant Collagen-mRNA Platform for Controllable Protein Synthesis

Significance Statement

Israel and Chinese researchers developed a collagen-mRNA platform for controllable protein production by designing a recombinant collagen mimic as scaffold for translating mRNA chains to proteins. Cysteines were genetically inserted into the collagen chain in positions allowing efficient ribosome translation activity while minimizing mRNA misfolding and degradation. Enhanced green fluorescence protein (eGFP) mRNA bound to collagen was successfully translated by cell-free E. coli ribosomes. This system enabled an accurate control of specific protein synthesis by monitoring expression time and level. Moreover, luciferase-mRNA was translated on this collagen scaffold by eukaryotic cell extracts. Since this platform enables accurate control of the types and amounts of specific proteins by the selection of the required mRNA sequence, expression time and expression level, it could provide an efficient local protein synthesis platform for wound areas, deficient tissues or damaged organs to promote tissue repair.

About The Author

Prof. Dr. Ada Yonath is the Director of the Helen and Milton A. Kimmelman Center for Biomolecular Structure and Assembly of Weizmann Institute of Science, Israel. In 2009 she received the Nobel Prize in Chemistry for her studies on the structure and function of the ribosome. Among her original scientific contributions, she introduced a novel technique, cryo bio-crystallography, which became routine and revolutionized structural biology worldwide. 

About The Author

Liping Sun is an associate Professor of the Biomaterials department at the Xiamen University, China. She carried out her postgraduate work in Prof. Ada Yonath’s group in Weizmann Institute of Science during 2011-2013. Her current research theme is dedicated to nanotechnology in medical diagnosis and treatment. 

Journal Reference

Chembiochem. 2015 Jul 6;16(10):1415-9.

Sun L1, Xiong Y1, Bashan A2, Zimmerman E2, Shulman Daube S2, Peleg Y2, Albeck S2, Unger T2, Yonath H3,4, Krupkin M2, Matzov D2, Yonath A5.

Show Affiliations
  1. Department of Biomaterials, College of Materials, Xiamen University, 422, Siming South Road, Xiamen 361005 (China).
  2. Weizmann Institute of Science, 234 Herzl Street, Rehovot 7610001 (Israel).
  3. Sheba Medical Center, 1 Sheba Street, Tel Hashomer 52621 (Israel).
  4. Sackler School of Medicine, Tel Aviv University, 10 Levanon Street, Tel Aviv 69978 (Israel).
  5. Weizmann Institute of Science, 234 Herzl Street, Rehovot 7610001 (Israel). [email protected]

Abstract

We have developed a collagen-mRNA platform for controllable protein production that is intended to be less prone to the problems associated with commonly used mRNA therapy as well as with collagen skin-healing procedures. A collagen mimic was constructed according to a recombinant method and was used as scaffold for translating mRNA chains into proteins. Cysteines were genetically inserted into the collagen chain at positions allowing efficient ribosome translation activity while minimizing mRNA misfolding and degradation. Enhanced green fluorescence protein (eGFP) mRNA bound to collagen was successfully translated by cell-free Escherichia coli ribosomes. This system enabled an accurate control of specific protein synthesis by monitoring expression time and level. Luciferase-mRNA was also translated on collagen scaffold by eukaryotic cell extracts. Thus we have demonstrated the feasibility of  controllable protein synthesis on collagen scaffolds by ribosomal machinery.
© 2015 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.

Go To Chembiochem.

Recombinant Collagen-mRNA Platform for Controllable Protein Synthesis. Global Medical Discovery

Figure legend
The ribosomal biosynthetic machinery on collagen-mRNA platform. Purple strands indicates mRNA, blue particles are ribosomes, and red spots are cysteines on the collagen triple helix strands. Green shiny strands are synthesized green fluorescence protein.