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Packaging guest proteins into the encapsulin nanocompartment from Rhodococcus erythropolis N771
Author(s) -
Tamura Akio,
Fukutani Yosuke,
Takami Taku,
Fujii Motoko,
Nakaguchi Yuki,
Murakami Yoshihiko,
Noguchi Keiichi,
Yohda Masafumi,
Odaka Masafumi
Publication year - 2015
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.25322
Subject(s) - dynamic light scattering , monomer , chemistry , particle (ecology) , biophysics , materials science , nanotechnology , polymer , nanoparticle , biology , organic chemistry , ecology
The encapsulin nanocompartment from Rhodococcus erythropolis N771 ( Re encapsulin) 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 Re encapsulin 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 Re encapsulin nanocompartment by fusing the C‐terminal 37‐amino‐acid sequence of the R. erythropolis N771 DypB peroxidase to the C‐terminus. Re encapsulin 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. Biotechnol. Bioeng. 2015;112: 13–20. © 2014 Wiley Periodicals, Inc.