Packaging Guest Proteins into the Encapsulin Nanocompartment from Rhodococcus erythropolis N771

作者：Tamura Akio; Fukutani Yosuke; Takami Taku; Fujii Motoko; Nakaguchi Yuki; Murakami Yoshihiko; Noguchi Keiichi; Yohda Masafumi; Odaka Masafumi^*

来源：Biotechnology and Bioengineering, 2015, 112(1): 13-20.

DOI：10.1002/bit.25322

• bacterial nanocompartment
• protein nanoparticle
• encapsulin
• DypB peroxidase
• nanobiotechnology

The encapsulin nanocompartment from Rhodococcus erythropolis N771 (Reencapsulin) was expressed and purified in wild-type and C-terminally His-tagged forms. Negative-stained transmission electron microscopy, field-flow fractionation combined with multi-angle light scattering and dynamic light scattering analyses showed that 60 Reencapsulin monomers were assembled as a spherical particle with a diameter of 28 nm. Heterogeneous guest proteins such as EGFP and firefly luciferase were packaged into the internal cavity of the Reencapsulin nanocompartment by fusing the C-terminal 37-amino-acid sequence of the R. erythropolis N771 DypB peroxidase to the C-terminus. Reencapsulin has the potential to package target proteins in its internal cavity and/or display them on its external surface, making it a feasible carrier for nanotechnology applications.

• 出版日期2015-1