ArticlePloS one2013
Recombinant production of human Aquaporin-1 to an exceptional high membrane density in Saccharomyces cerevisiae.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 38 citations in OpenAlex.
- Direct observation of fluorescent proteins in gels: A rapid, cost-efficient, and quantitative alternative to immunoblotting.Biology of the cell · 2025Article
- Proteoliposomes reconstituted with human aquaporin-1 reveal novel single-ion-channel properties.Biophysical reports · 2023Article
- pXOOY: A dual-function vector for expression of membrane proteins in Saccharomyces cerevisiae and Xenopus laevis oocytes.PloS one · 2023Article
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- Production of an Active, Human Membrane Protein inInternational journal of molecular sciences · 2022Article
- Article
- Characterization of Hailey-Hailey Disease-mutants in presence and absence of wild type SPCA1 using Saccharomyces cerevisiae as model organism.Scientific reports · 2019Article
- Article
- Review
- Purification and functional comparison of nine human Aquaporins produced in Saccharomyces cerevisiae for the purpose of biophysical characterization.Scientific reports · 2017Article
- Characterization of ATP7A missense mutants suggests a correlation between intracellular trafficking and severity of Menkes disease.Scientific reports · 2017Article
- Challenges in Commercializing Biomimetic Membranes.Membranes · 2015Review
- Can Stabilization and Inhibition of Aquaporins Contribute to Future Development of Biomimetic Membranes?Membranes · 2015Review
- High yield purification of full-length functional hERG K+ channels produced in Saccharomyces cerevisiae.Microbial cell factories · 2015Article
- Crystallization and preliminary crystallographic analysis of human aquaporin 1 at a resolution of 3.28 Å.Acta crystallographica. Section F, Structural biology communications · 2014Article
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Authors and funding
4 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
In the present paper we explored the capacity of yeast Saccharomyces cerevisiae as host for heterologous expression of human Aquaporin-1. Aquaporin-1 cDNA was expressed from a galactose inducible promoter situated on a plasmid with an adjustable copy number. Human Aquaporin-1 was C-terminally tagged with yeast enhanced GFP for quantification of functional expression, determination of sub-cellular localization, estimation of in vivo folding efficiency and establishment of a purification protocol. Aquaporin-1 was found to constitute 8.5 percent of total membrane protein content after expression at 15°C in a yeast host over-producing the Gal4p transcriptional activator and growth in amino acid supplemented minimal medium. In-gel fluorescence combined with western blotting showed that low accumulation of correctly folded recombinant Aquaporin-1 at 30°C was due to in vivo mal-folding. Reduction of the expression temperature to 15°C almost completely prevented Aquaporin-1 mal-folding. Bioimaging of live yeast cells revealed that recombinant Aquaporin-1 accumulated in the yeast plasma membrane. A detergent screen for solubilization revealed that CYMAL-5 was superior in solubilizing recombinant Aquaporin-1 and generated a monodisperse protein preparation. A single Ni-affinity chromatography step was used to obtain almost pure Aquaporin-1. Recombinant Aquaporin-1 produced in S. cerevisiae was not N-glycosylated in contrast to the protein found in human erythrocytes.
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