Ethanolamine bacterial microcompartments: from structure, function studies to bioengineering applications

Anaya Pokhrel; Sun young Kang; Claudia Schmidt-Dannert

doi:10.1016/j.mib.2021.04.008

Ethanolamine bacterial microcompartments: from structure, function studies to bioengineering applications

Anaya Pokhrel, Sun young Kang, Claudia Schmidt-Dannert

Research output: Contribution to journal › Review article › peer-review

6 Scopus citations

Abstract

Two decades of structural and functional studies have revealed functions, structures and diversity of bacterial microcompartments. The protein-based organelles encapsulate diverse metabolic pathways in semipermeable, icosahedral or pseudo-icosahedral shells. One of the first discovered and characterized microcompartments are those involved in ethanolamine degradation. This review will summarize their function and assembly along with shared and unique characteristics with other microcompartment types. The modularity and self-assembling properties of their shell proteins make them valuable targets for bioengineering. Advances and prospects for shell protein engineering in vivo and in vitro for synthetic biology and biotechnology applications will be discussed.

Original language	English (US)
Pages (from-to)	28-37
Number of pages	10
Journal	Current Opinion in Microbiology
Volume	62
DOIs	https://doi.org/10.1016/j.mib.2021.04.008
State	Published - Aug 2021

Bibliographical note

Funding Information:
Research on the development of self-assembling protein materials in the Schmidt-Dannert Laboratory have been supported by Defense Threat Reduction Agency Grant HDTRA-15-0004 , Defense Advanced Research Projects Agency Contract HR0011-17-0038 , National Science Foundation Grant CBET-1916030 , MnDRIVE and the University of Minnesota’s Biocatalysis Initiative .

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© 2021 Elsevier Ltd

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title = "Ethanolamine bacterial microcompartments: from structure, function studies to bioengineering applications",

abstract = "Two decades of structural and functional studies have revealed functions, structures and diversity of bacterial microcompartments. The protein-based organelles encapsulate diverse metabolic pathways in semipermeable, icosahedral or pseudo-icosahedral shells. One of the first discovered and characterized microcompartments are those involved in ethanolamine degradation. This review will summarize their function and assembly along with shared and unique characteristics with other microcompartment types. The modularity and self-assembling properties of their shell proteins make them valuable targets for bioengineering. Advances and prospects for shell protein engineering in vivo and in vitro for synthetic biology and biotechnology applications will be discussed.",

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AU - Pokhrel, Anaya

AU - Kang, Sun young

AU - Schmidt-Dannert, Claudia

N1 - Funding Information: Research on the development of self-assembling protein materials in the Schmidt-Dannert Laboratory have been supported by Defense Threat Reduction Agency Grant HDTRA-15-0004 , Defense Advanced Research Projects Agency Contract HR0011-17-0038 , National Science Foundation Grant CBET-1916030 , MnDRIVE and the University of Minnesota’s Biocatalysis Initiative . Publisher Copyright: © 2021 Elsevier Ltd

PY - 2021/8

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N2 - Two decades of structural and functional studies have revealed functions, structures and diversity of bacterial microcompartments. The protein-based organelles encapsulate diverse metabolic pathways in semipermeable, icosahedral or pseudo-icosahedral shells. One of the first discovered and characterized microcompartments are those involved in ethanolamine degradation. This review will summarize their function and assembly along with shared and unique characteristics with other microcompartment types. The modularity and self-assembling properties of their shell proteins make them valuable targets for bioengineering. Advances and prospects for shell protein engineering in vivo and in vitro for synthetic biology and biotechnology applications will be discussed.

AB - Two decades of structural and functional studies have revealed functions, structures and diversity of bacterial microcompartments. The protein-based organelles encapsulate diverse metabolic pathways in semipermeable, icosahedral or pseudo-icosahedral shells. One of the first discovered and characterized microcompartments are those involved in ethanolamine degradation. This review will summarize their function and assembly along with shared and unique characteristics with other microcompartment types. The modularity and self-assembling properties of their shell proteins make them valuable targets for bioengineering. Advances and prospects for shell protein engineering in vivo and in vitro for synthetic biology and biotechnology applications will be discussed.

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Ethanolamine bacterial microcompartments: from structure, function studies to bioengineering applications

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