ArticleApplied and environmental microbiology2004
Assembly of G protein-coupled receptors onto nanosized bacterial magnetic particles using Mms16 as an anchor molecule.
Article in Applied and environmental microbiology, 2004. 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.
- OrthogonalApplied and environmental microbiology · 2025Article
- Functional expression of full-length TrkA in the prokaryotic host Magnetospirillum magneticum AMB-1 by using a magnetosome display system.Applied and environmental microbiology · 2015Article
- New vectors for chromosomal integration enable high-level constitutive or inducible magnetosome expression of fusion proteins in Magnetospirillum gryphiswaldense.Applied and environmental microbiology · 2014Article
- Functional expression of thyroid-stimulating hormone receptor on nano-sized bacterial magnetic particles in Magnetospirillum magneticum AMB-1.International journal of molecular sciences · 2013Article
- Geobacillus thermoglucosidasius endospores function as nuclei for the formation of single calcite crystals.Applied and environmental microbiology · 2013Article
- Relevant uses of surface proteins--display on self-organized biological structures.Microbial biotechnology · 2012Review
- MMS6 protein regulates crystal morphology during nano-sized magnetite biomineralization in vivo.The Journal of biological chemistry · 2011Article
- In vivo biotinylation of bacterial magnetic particles by a truncated form of Escherichia coli biotin ligase and biotin acceptor peptide.Applied and environmental microbiology · 2010Article
- Inducible expression of transmembrane proteins on bacterial magnetic particles in Magnetospirillum magneticum AMB-1.Applied and environmental microbiology · 2010Article
- In vivo display of a multisubunit enzyme complex on biogenic magnetic nanoparticles.Applied and environmental microbiology · 2009Article
- Novel method for selection of antimicrobial peptides from a phage display library by use of bacterial magnetic particles.Applied and environmental microbiology · 2008Article
- Formation of magnetite by bacteria and its application.Journal of the Royal Society, Interface · 2008Review
- Expression of green fluorescent protein fused to magnetosome proteins in microaerophilic magnetotactic bacteria.Applied and environmental microbiology · 2008Article
- Development of a cell surface display system in a magnetotactic bacterium, "Magnetospirillum magneticum" AMB-1.Applied and environmental microbiology · 2008Article
- Efficient and stable display of functional proteins on bacterial magnetic particles using mms13 as a novel anchor molecule.Applied and environmental microbiology · 2006Article
- The presumptive magnetosome protein Mms16 is a poly(3-hydroxybutyrate) granule-bound protein (phasin) in Magnetospirillum gryphiswaldense.Journal of bacteriology · 2005Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
G protein-coupled receptors (GPCRs) play a central role in a wide range of biological processes and are prime targets for drug discovery. GPCRs have large hydrophobic domains, and therefore purification of GPCRs from cells is frequently time-consuming and typically results in loss of native conformation. In this work, GPCRs have been successfully assembled into the lipid membrane of nanosized bacterial magnetic particles (BMPs) produced by the magnetic bacterium Magnetospirillum magneticum AMB-1. A BMP-specific protein, Mms16, was used as an anchor molecule, and localization of heterologous Mms16 on BMPs was confirmed by luciferase fusion studies. Stable luminescence was obtained from BMPs bearing Mms16 fused with luciferase at the C-terminal region. D1 dopamine receptor (D1R), a GPCR, was also efficiently assembled onto BMPs by using Mms16 as an anchor molecule. D1R-BMP complexes were simply extracted by magnetic separation from ruptured AMB-1 transformants. After washing, the complexes were ready to use for analysis. This system conveniently refines the native conformation of GPCRs without the need for detergent solubilization, purification, and reconstitution after cell disruption.
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