In vivo display of a multisubunit enzyme complex on biogenic magnetic nanoparticles.
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) of Escherichia coli RNase P and the endogenous RNA subunit by expressing a translational fusion of C5 with MamC, a known magnetosome protein, in the magnetotactic bacterium Magnetospirillum 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.
Ohuchi
Shoji
S
Department of Basic Medical Sciences, Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan. sohuchi@ims.u-tokyo.ac.jp
Schüler
Dirk
D
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D001483:Base Sequence; D001671:Biochemistry / Q000379:methods*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D055944:Magnetosomes; D042201:Magnetospirillum / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000737:chemistry*; D012329:RNA, Bacterial / Q000737:chemistry; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D043262:Ribonuclease P / Q000737:chemistry*
D001426:Bacterial Proteins; D009097:Multienzyme Complexes; D012329:RNA, Bacterial; D011993:Recombinant Fusion Proteins; D043262:Ribonuclease P