Packaging guest proteins into the encapsulin nanocompartment from Rhodococcus erythropolis N771.

Abstract:

: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.

journal_name

Biotechnol Bioeng

authors

Tamura A,Fukutani Y,Takami T,Fujii M,Nakaguchi Y,Murakami Y,Noguchi K,Yohda M,Odaka M

doi

10.1002/bit.25322

subject

Has Abstract

pub_date

2015-01-01 00:00:00

pages

13-20

issue

1

eissn

0006-3592

issn

1097-0290

journal_volume

112

pub_type

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