Cell-free methods to produce structurally intact mammalian membrane proteins View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-09

AUTHORS

Takehiro Shinoda, Naoko Shinya, Kaori Ito, Yoshiko Ishizuka-Katsura, Noboru Ohsawa, Takaho Terada, Kunio Hirata, Yoshiaki Kawano, Masaki Yamamoto, Taisuke Tomita, Yohei Ishibashi, Yoshio Hirabayashi, Tomomi Kimura-Someya, Mikako Shirouzu, Shigeyuki Yokoyama

ABSTRACT

The crystal structures of four membrane proteins, from bacteria or a unicellular alga, have been solved with samples produced by cell-free protein synthesis. In this study, for mammalian membrane protein production, we established the precipitating and soluble membrane fragment methods: membrane proteins are synthesized with the Escherichia coli cell-free system in the presence of large and small membrane fragments, respectively, and are simultaneously integrated into the lipid environments. We applied the precipitating membrane fragment method to produce various mammalian membrane proteins, including human claudins, glucosylceramide synthase, and the γ-secretase subunits. These proteins were produced at levels of about 0.1-1.0 mg per ml cell-free reaction under the initial conditions, and were obtained as precipitates by ultracentrifugation. Larger amounts of membrane proteins were produced by the soluble membrane fragment method, collected in the ultracentrifugation supernatants, and purified directly by column chromatography. For several proteins, the conditions of the membrane fragment methods were further optimized, such as by the addition of specific lipids/detergents. The functional and structural integrities of the purified proteins were confirmed by analyses of their ligand binding activities, size-exclusion chromatography profiles, and/or thermal stabilities. We successfully obtained high-quality crystals of the complex of human claudin-4 with an enterotoxin. More... »

PAGES

30442

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/srep30442

DOI

http://dx.doi.org/10.1038/srep30442

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1029400865

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27465719


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