In vitro assembly of bacterial microcompartments
Abstract
The present disclosure is related to a BMC fusion protein that is capable of in vitro assembly, comprising a constituent BMC shell protein subunit and a sterically hindering protein domain that is cleavable. The BMC fusion protein is capable of in vitro assembly triggered by removal of the fused sterically hindering domain. The present disclosure is also related to a means to produce BMC shells in vitro, triggered by removal of a fused sterically hindering domain from one or more constituent BMC shell protein subunits. The BMC fusion protein enables encapsulation of broad classes of materials and biophysical studies of shell assembly, encapsulation, and permeability that would otherwise be unavailable from BMCs assembled in vivo.
- Inventors:
- Issue Date:
- Research Org.:
- Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1805489
- Patent Number(s):
- 10913777
- Application Number:
- 15/985,218
- Assignee:
- The Regents of the University of California (Oakland, CA)
- DOE Contract Number:
- AC02-05CH11231; FG02-91ER20021
- Resource Type:
- Patent
- Resource Relation:
- Patent File Date: 05/21/2018
- Country of Publication:
- United States
- Language:
- English
Citation Formats
Hagen, Andrew Ronald, Kerfeld, Cheryl A., and Sutter, Markus. In vitro assembly of bacterial microcompartments. United States: N. p., 2021.
Web.
Hagen, Andrew Ronald, Kerfeld, Cheryl A., & Sutter, Markus. In vitro assembly of bacterial microcompartments. United States.
Hagen, Andrew Ronald, Kerfeld, Cheryl A., and Sutter, Markus. Tue .
"In vitro assembly of bacterial microcompartments". United States. https://www.osti.gov/servlets/purl/1805489.
@article{osti_1805489,
title = {In vitro assembly of bacterial microcompartments},
author = {Hagen, Andrew Ronald and Kerfeld, Cheryl A. and Sutter, Markus},
abstractNote = {The present disclosure is related to a BMC fusion protein that is capable of in vitro assembly, comprising a constituent BMC shell protein subunit and a sterically hindering protein domain that is cleavable. The BMC fusion protein is capable of in vitro assembly triggered by removal of the fused sterically hindering domain. The present disclosure is also related to a means to produce BMC shells in vitro, triggered by removal of a fused sterically hindering domain from one or more constituent BMC shell protein subunits. The BMC fusion protein enables encapsulation of broad classes of materials and biophysical studies of shell assembly, encapsulation, and permeability that would otherwise be unavailable from BMCs assembled in vivo.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {2021},
month = {2}
}