Open AccessIn Vivo Display of a Multisubunit Enzyme Complex on Biogenic Magnetic Nanoparticles
Author(s) -
Shoji Ohuchi,
Dirk Schüler
Publication year - 2009
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.01640-09
Subject(s) - magnetosome , magnetotactic bacteria , rnase p , organelle , protein subunit , biology , rna , fusion protein , escherichia coli , microbiology and biotechnology , chemistry , biochemistry , bacteria , recombinant dna , genetics , gene
Magnetosomes are unique bacterial organelles comprising membrane-enveloped magnetic crystals produced by magnetotactic bacteria. Because of several desirable chemical and physical properties, magnetosomes would be ideal scaffolds on which to display highly complicated biological complexes artificially. As a model experiment for the functional expression of a multisubunit complex on magnetosomes, we examined the display of a chimeric bacterial RNase P enzyme composed of the protein subunit (C5) ofEscherichia coli RNase P and the endogenous RNA subunit by expressing a translational fusion of C5 with MamC, a known magnetosome protein, in the magnetotactic bacteriumMagnetospirillum gryphiswaldense . As intended, the purified C5 fusion magnetosomes, but not wild-type magnetosomes, showed apparent RNase P activity and the association of a typical bacterial RNase P RNA. Our results demonstrate for the first time that magnetosomes can be employed as scaffolds for the display of multisubunit complexes.