The encapsulin from Thermotoga maritima is a flavoprotein with a symmetry matched ferritin-like cargo protein

Abstract Bacterial nanocompartments, also known as encapsulins, are an emerging class of protein-based ‘organelles’ found in bacteria and archaea. Encapsulins are virus-like icosahedral particles comprising a ~ 25–50 nm shell surrounding a specific cargo enzyme. Compartmentalization is thought to cr...

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Autores principales:	Benjamin J. LaFrance, Caleb Cassidy-Amstutz, Robert J. Nichols, Luke M. Oltrogge, Eva Nogales, David F. Savage
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/02ef4047d2ff45de8942231742dab155
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spelling	oai:doaj.org-article:02ef4047d2ff45de8942231742dab1552021-11-28T12:20:56ZThe encapsulin from Thermotoga maritima is a flavoprotein with a symmetry matched ferritin-like cargo protein10.1038/s41598-021-01932-w2045-2322https://doaj.org/article/02ef4047d2ff45de8942231742dab1552021-11-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-01932-whttps://doaj.org/toc/2045-2322Abstract Bacterial nanocompartments, also known as encapsulins, are an emerging class of protein-based ‘organelles’ found in bacteria and archaea. Encapsulins are virus-like icosahedral particles comprising a ~ 25–50 nm shell surrounding a specific cargo enzyme. Compartmentalization is thought to create a unique chemical environment to facilitate catalysis and isolate toxic intermediates. Many questions regarding nanocompartment structure–function remain unanswered, including how shell symmetry dictates cargo loading and to what extent the shell facilitates enzymatic activity. Here, we explore these questions using the model Thermotoga maritima nanocompartment known to encapsulate a redox-active ferritin-like protein. Biochemical analysis revealed the encapsulin shell to possess a flavin binding site located at the interface between capsomere subunits, suggesting the shell may play a direct and active role in the function of the encapsulated cargo. Furthermore, we used cryo-EM to show that cargo proteins use a form of symmetry-matching to facilitate encapsulation and define stoichiometry. In the case of the Thermotoga maritima encapsulin, the decameric cargo protein with fivefold symmetry preferentially binds to the pentameric-axis of the icosahedral shell. Taken together, these observations suggest the shell is not simply a passive barrier—it also plays a significant role in the structure and function of the cargo enzyme.Benjamin J. LaFranceCaleb Cassidy-AmstutzRobert J. NicholsLuke M. OltroggeEva NogalesDavid F. SavageNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Benjamin J. LaFrance Caleb Cassidy-Amstutz Robert J. Nichols Luke M. Oltrogge Eva Nogales David F. Savage The encapsulin from Thermotoga maritima is a flavoprotein with a symmetry matched ferritin-like cargo protein
description	Abstract Bacterial nanocompartments, also known as encapsulins, are an emerging class of protein-based ‘organelles’ found in bacteria and archaea. Encapsulins are virus-like icosahedral particles comprising a ~ 25–50 nm shell surrounding a specific cargo enzyme. Compartmentalization is thought to create a unique chemical environment to facilitate catalysis and isolate toxic intermediates. Many questions regarding nanocompartment structure–function remain unanswered, including how shell symmetry dictates cargo loading and to what extent the shell facilitates enzymatic activity. Here, we explore these questions using the model Thermotoga maritima nanocompartment known to encapsulate a redox-active ferritin-like protein. Biochemical analysis revealed the encapsulin shell to possess a flavin binding site located at the interface between capsomere subunits, suggesting the shell may play a direct and active role in the function of the encapsulated cargo. Furthermore, we used cryo-EM to show that cargo proteins use a form of symmetry-matching to facilitate encapsulation and define stoichiometry. In the case of the Thermotoga maritima encapsulin, the decameric cargo protein with fivefold symmetry preferentially binds to the pentameric-axis of the icosahedral shell. Taken together, these observations suggest the shell is not simply a passive barrier—it also plays a significant role in the structure and function of the cargo enzyme.
format	article
author	Benjamin J. LaFrance Caleb Cassidy-Amstutz Robert J. Nichols Luke M. Oltrogge Eva Nogales David F. Savage
author_facet	Benjamin J. LaFrance Caleb Cassidy-Amstutz Robert J. Nichols Luke M. Oltrogge Eva Nogales David F. Savage
author_sort	Benjamin J. LaFrance
title	The encapsulin from Thermotoga maritima is a flavoprotein with a symmetry matched ferritin-like cargo protein
title_short	The encapsulin from Thermotoga maritima is a flavoprotein with a symmetry matched ferritin-like cargo protein
title_full	The encapsulin from Thermotoga maritima is a flavoprotein with a symmetry matched ferritin-like cargo protein
title_fullStr	The encapsulin from Thermotoga maritima is a flavoprotein with a symmetry matched ferritin-like cargo protein
title_full_unstemmed	The encapsulin from Thermotoga maritima is a flavoprotein with a symmetry matched ferritin-like cargo protein
title_sort	encapsulin from thermotoga maritima is a flavoprotein with a symmetry matched ferritin-like cargo protein
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/02ef4047d2ff45de8942231742dab155
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The encapsulin from Thermotoga maritima is a flavoprotein with a symmetry matched ferritin-like cargo protein

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