Exploring targeting peptide-shell interactions in encapsulin nanocompartments

Abstract Encapsulins are recently discovered protein compartments able to specifically encapsulate cargo proteins in vivo. Encapsulation is dependent on C-terminal targeting peptides (TPs). Here, we characterize and engineer TP-shell interactions in the Thermotoga maritima and Myxococcus xanthus enc...

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Autores principales:	Wiggert J. Altenburg, Nathan Rollins, Pamela A. Silver, Tobias W. Giessen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/91c356a784e24cafbcf78672c4a1ab34
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spelling	oai:doaj.org-article:91c356a784e24cafbcf78672c4a1ab342021-12-02T11:37:22ZExploring targeting peptide-shell interactions in encapsulin nanocompartments10.1038/s41598-021-84329-z2045-2322https://doaj.org/article/91c356a784e24cafbcf78672c4a1ab342021-03-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-84329-zhttps://doaj.org/toc/2045-2322Abstract Encapsulins are recently discovered protein compartments able to specifically encapsulate cargo proteins in vivo. Encapsulation is dependent on C-terminal targeting peptides (TPs). Here, we characterize and engineer TP-shell interactions in the Thermotoga maritima and Myxococcus xanthus encapsulin systems. Using force-field modeling and particle fluorescence measurements we show that TPs vary in native specificity and binding strength, and that TP-shell interactions are determined by hydrophobic and ionic interactions as well as TP flexibility. We design a set of TPs with a variety of predicted binding strengths and experimentally characterize these designs. This yields a set of TPs with novel binding characteristics representing a potentially useful toolbox for future nanoreactor engineering aimed at controlling cargo loading efficiency and the relative stoichiometry of multiple concurrently loaded cargo proteins.Wiggert J. AltenburgNathan RollinsPamela A. SilverTobias W. GiessenNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-9 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Wiggert J. Altenburg Nathan Rollins Pamela A. Silver Tobias W. Giessen Exploring targeting peptide-shell interactions in encapsulin nanocompartments
description	Abstract Encapsulins are recently discovered protein compartments able to specifically encapsulate cargo proteins in vivo. Encapsulation is dependent on C-terminal targeting peptides (TPs). Here, we characterize and engineer TP-shell interactions in the Thermotoga maritima and Myxococcus xanthus encapsulin systems. Using force-field modeling and particle fluorescence measurements we show that TPs vary in native specificity and binding strength, and that TP-shell interactions are determined by hydrophobic and ionic interactions as well as TP flexibility. We design a set of TPs with a variety of predicted binding strengths and experimentally characterize these designs. This yields a set of TPs with novel binding characteristics representing a potentially useful toolbox for future nanoreactor engineering aimed at controlling cargo loading efficiency and the relative stoichiometry of multiple concurrently loaded cargo proteins.
format	article
author	Wiggert J. Altenburg Nathan Rollins Pamela A. Silver Tobias W. Giessen
author_facet	Wiggert J. Altenburg Nathan Rollins Pamela A. Silver Tobias W. Giessen
author_sort	Wiggert J. Altenburg
title	Exploring targeting peptide-shell interactions in encapsulin nanocompartments
title_short	Exploring targeting peptide-shell interactions in encapsulin nanocompartments
title_full	Exploring targeting peptide-shell interactions in encapsulin nanocompartments
title_fullStr	Exploring targeting peptide-shell interactions in encapsulin nanocompartments
title_full_unstemmed	Exploring targeting peptide-shell interactions in encapsulin nanocompartments
title_sort	exploring targeting peptide-shell interactions in encapsulin nanocompartments
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/91c356a784e24cafbcf78672c4a1ab34
work_keys_str_mv	AT wiggertjaltenburg exploringtargetingpeptideshellinteractionsinencapsulinnanocompartments AT nathanrollins exploringtargetingpeptideshellinteractionsinencapsulinnanocompartments AT pamelaasilver exploringtargetingpeptideshellinteractionsinencapsulinnanocompartments AT tobiaswgiessen exploringtargetingpeptideshellinteractionsinencapsulinnanocompartments
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Exploring targeting peptide-shell interactions in encapsulin nanocompartments

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