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Title: Purification and Characterization of Protein Nanotubes Assembled from a Single Bacterial Microcompartment Shell Subunit

Abstract

Bacterial microcompartments (BMCs) are apparently icosahedral proteinaceous organelles that are bioinformatically identified in an increasing number of bacterial species. BMCs are delimited by a protein shell composed predominantly of hexameric (BMC-H) subunits that tile into the facets of the BMC shell. Here we report a new biomaterial composed of the single BMC-H protein encoded in the BMC locus of Mycobacterium smegmatis; the function of this type of BMC is unknown. When expressed in Escherichia coli, this BMC-H protein, RmmH, self-assembles into nanotubes, densely packed in the cytoplasmic space. These are the first BMC nanotubes to be purified from cells intact and characterized. Here, we also show formation of the nanotubes initiated from free RmmH hexamers in vitro. Based on the dimensions of the nanotubes and modeling of the RmmH hexamer, we propose two possible structural models. BMC nanotubes offer a new spatial architecture both in vivo and in vitro, composed of a single protein that may be genetically or chemically modified and for use as tubular scaffolding.

Authors:
 [1];  [2];  [3]
  1. Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Lab.
  2. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
  3. Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Lab.; Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States); Univ. of California, Berkeley, CA (United States)
Publication Date:
Research Org.:
Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory
Sponsoring Org.:
USDOE Office of Science (SC), Advanced Scientific Computing Research (ASCR). Scientific Discovery through Advanced Computing (SciDAC); USDOE Office of Science (SC), Basic Energy Sciences (BES)
OSTI Identifier:
1714342
Grant/Contract Number:  
FG02-91ER20021
Resource Type:
Accepted Manuscript
Journal Name:
Advanced Materials Interfaces
Additional Journal Information:
Journal Volume: 3; Journal Issue: 1; Journal ID: ISSN 2196-7350
Publisher:
Wiley-VCH
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; nanotube; bacterial microcompartment; Mycobacterium smegmatis; scaffold; nanotechnology

Citation Formats

Noël, Christopher R., Cai, Fei, and Kerfeld, Cheryl A. Purification and Characterization of Protein Nanotubes Assembled from a Single Bacterial Microcompartment Shell Subunit. United States: N. p., 2015. Web. doi:10.1002/admi.201500295.
Noël, Christopher R., Cai, Fei, & Kerfeld, Cheryl A. Purification and Characterization of Protein Nanotubes Assembled from a Single Bacterial Microcompartment Shell Subunit. United States. https://doi.org/10.1002/admi.201500295
Noël, Christopher R., Cai, Fei, and Kerfeld, Cheryl A. Thu . "Purification and Characterization of Protein Nanotubes Assembled from a Single Bacterial Microcompartment Shell Subunit". United States. https://doi.org/10.1002/admi.201500295. https://www.osti.gov/servlets/purl/1714342.
@article{osti_1714342,
title = {Purification and Characterization of Protein Nanotubes Assembled from a Single Bacterial Microcompartment Shell Subunit},
author = {Noël, Christopher R. and Cai, Fei and Kerfeld, Cheryl A.},
abstractNote = {Bacterial microcompartments (BMCs) are apparently icosahedral proteinaceous organelles that are bioinformatically identified in an increasing number of bacterial species. BMCs are delimited by a protein shell composed predominantly of hexameric (BMC-H) subunits that tile into the facets of the BMC shell. Here we report a new biomaterial composed of the single BMC-H protein encoded in the BMC locus of Mycobacterium smegmatis; the function of this type of BMC is unknown. When expressed in Escherichia coli, this BMC-H protein, RmmH, self-assembles into nanotubes, densely packed in the cytoplasmic space. These are the first BMC nanotubes to be purified from cells intact and characterized. Here, we also show formation of the nanotubes initiated from free RmmH hexamers in vitro. Based on the dimensions of the nanotubes and modeling of the RmmH hexamer, we propose two possible structural models. BMC nanotubes offer a new spatial architecture both in vivo and in vitro, composed of a single protein that may be genetically or chemically modified and for use as tubular scaffolding.},
doi = {10.1002/admi.201500295},
journal = {Advanced Materials Interfaces},
number = 1,
volume = 3,
place = {United States},
year = {Thu Oct 08 00:00:00 EDT 2015},
month = {Thu Oct 08 00:00:00 EDT 2015}
}

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