Journal
PROTEIN EXPRESSION AND PURIFICATION
Volume 43, Issue 1, Pages 1-9Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pep.2005.03.016
Keywords
protein expression; gene fusion; protein fusion; ubhiquitin; SUMO; ubiquitin-like proteins
Categories
Funding
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R43HL069744] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R43AI058584, R43AI051752] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R43GM067271, R43GM068404] Funding Source: NIH RePORTER
- NHLBI NIH HHS [R43 HL 69744] Funding Source: Medline
- NIAID NIH HHS [R43 AI058584, 1R43-AI058584-01A1, R43 AI 51752] Funding Source: Medline
- NIGMS NIH HHS [R43 GM 067271, R43 GM 068404, R43 GM067271, R43 GM068404] Funding Source: Medline
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The demands of structural and functional genomics for large quantities of soluble, properly folded proteins in heterologous hosts have been aided by advancements in the field of protein production and purification. Escherichia coli, the preferred host for recombinant protein expression, presents many challenges which must be surmounted in order to over-express heterologous proteins. These challenges include the proteolytic degradation of target proteins, protein misfolding, poor solubility, and the necessity for good purification methodologies. Gene fusion technologies have been able to, improve heterologous expression by overcoming many of these challenges. The ability of gene fusions to improve expression, solubility, purification, and decrease proteolytic degradation will be discussed in this review. The main disadvantage, cleaving the protein fusion, will also be addressed. Focus will be given to the newly described SUMO fusion system and the improvements that this technology has advanced over traditional gene fusion systems. (c) 2005 Elsevier Inc. All rights reserved.
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