ArticleProtein expression and purification2011
A systematic assessment of mature MBP in membrane protein production: overexpression, membrane targeting and purification.
Article in Protein expression and purification, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 36 citations in OpenAlex.
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- Heme binding of transmembrane signaling proteins undergoing regulated intramembrane proteolysis.Communications biology · 2020Article
- High Yield Expression of Recombinant CD151 in E. coli and a Structural Insight into Cholesterol Binding Domain.Molecular biotechnology · 2019Article
- Construction and characterization of a transmembrane eukaryotic expression vector based on the membrane domain structure of TNF-α.Molecular medicine reports · 2017Article
- The MICOS component Mic60 displays a conserved membrane-bending activity that is necessary for normal cristae morphology.The Journal of cell biology · 2017Article
- A Novel and Fast Purification Method for Nucleoside Transporters.Frontiers in molecular biosciences · 2016Article
- Membrane protein structure from rotational diffusion.Biochimica et biophysica acta · 2015Review
- Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.Nature protocols · 2013Article
- Solid state NMR strategy for characterizing native membrane protein structures.Accounts of chemical research · 2013Article
- Strategies for the production of recombinant protein in Escherichia coli.The protein journal · 2013Review
- Expression and purification of the membrane enzyme selenoprotein K.Protein expression and purification · 2012Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Obtaining enough membrane protein in native or native-like status is still a challenge in membrane protein structure biology. Maltose binding protein (MBP) has been widely used as a fusion partner in improving membrane protein production. In the present work, a systematic assessment on the application of mature MBP (mMBP) for membrane protein overexpression and purification was performed on 42 membrane proteins, most of which showed no or poor expression level in membrane fraction fused with an N-terminal Histag. It was found that most of the small membrane proteins were overexpressed in the native membrane of Escherichia coli when using mMBP. In addition, the proteolysis of the fusions were performed on the membrane without solubilization with detergents, leading to the development of an efficient protocol to directly purify the target membrane proteins from the membrane fraction through a one-step affinity chromatography. Our results indicated that mMBP is an excellent fusion partner for overexpression, membrane targeting and purification of small membrane proteins. The present expression and purification method may be a good solution for the large scale preparation of small membrane proteins in structural and functional studies.
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