Crystal and solution structures reveal oligomerization of individual capsid homology domains of Drosophila Arc.

Synaptic plasticity is vital for brain function and memory formation. One of the key proteins in long-term synaptic plasticity and memory is the activity-regulated cytoskeleton-associated protein (Arc). Mammalian Arc forms virus-like capsid structures in a process requiring the N-terminal domain and...

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Autores principales:	Erik I Hallin, Sigurbjörn Markússon, Lev Böttger, Andrew E Torda, Clive R Bramham, Petri Kursula
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f34bcf4d31044cea8105ca392cd38f76
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spelling	oai:doaj.org-article:f34bcf4d31044cea8105ca392cd38f762021-12-02T20:04:00ZCrystal and solution structures reveal oligomerization of individual capsid homology domains of Drosophila Arc.1932-620310.1371/journal.pone.0251459https://doaj.org/article/f34bcf4d31044cea8105ca392cd38f762021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0251459https://doaj.org/toc/1932-6203Synaptic plasticity is vital for brain function and memory formation. One of the key proteins in long-term synaptic plasticity and memory is the activity-regulated cytoskeleton-associated protein (Arc). Mammalian Arc forms virus-like capsid structures in a process requiring the N-terminal domain and contains two C-terminal lobes that are structural homologues to retroviral capsids. Drosophila has two isoforms of Arc, dArc1 and dArc2, with low sequence similarity to mammalian Arc, but lacking a large N-terminal domain. Both dArc isoforms are related to the Ty3/gypsy retrotransposon capsid, consisting of N- and C-terminal lobes. Structures of dArc1, as well as capsids formed by both dArc isoforms, have been recently determined. We carried out structural characterization of the four individual dArc lobe domains. As opposed to the corresponding mammalian Arc lobe domains, which are monomeric, the dArc lobes were all oligomeric in solution, indicating a strong propensity for homophilic interactions. A truncated N-lobe from dArc2 formed a domain-swapped dimer in the crystal structure, resulting in a novel dimer interaction that could be relevant for capsid assembly or other dArc functions. This domain-swapped structure resembles the dimeric protein C of flavivirus capsids, as well as the structure of histones dimers, domain-swapped transcription factors, and membrane-interacting BAK domains. The strong oligomerization properties of the isolated dArc lobe domains explain the ability of dArc to form capsids in the absence of any large N-terminal domain, in contrast to the mammalian protein.Erik I HallinSigurbjörn MarkússonLev BöttgerAndrew E TordaClive R BramhamPetri KursulaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 5, p e0251459 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Erik I Hallin Sigurbjörn Markússon Lev Böttger Andrew E Torda Clive R Bramham Petri Kursula Crystal and solution structures reveal oligomerization of individual capsid homology domains of Drosophila Arc.
description	Synaptic plasticity is vital for brain function and memory formation. One of the key proteins in long-term synaptic plasticity and memory is the activity-regulated cytoskeleton-associated protein (Arc). Mammalian Arc forms virus-like capsid structures in a process requiring the N-terminal domain and contains two C-terminal lobes that are structural homologues to retroviral capsids. Drosophila has two isoforms of Arc, dArc1 and dArc2, with low sequence similarity to mammalian Arc, but lacking a large N-terminal domain. Both dArc isoforms are related to the Ty3/gypsy retrotransposon capsid, consisting of N- and C-terminal lobes. Structures of dArc1, as well as capsids formed by both dArc isoforms, have been recently determined. We carried out structural characterization of the four individual dArc lobe domains. As opposed to the corresponding mammalian Arc lobe domains, which are monomeric, the dArc lobes were all oligomeric in solution, indicating a strong propensity for homophilic interactions. A truncated N-lobe from dArc2 formed a domain-swapped dimer in the crystal structure, resulting in a novel dimer interaction that could be relevant for capsid assembly or other dArc functions. This domain-swapped structure resembles the dimeric protein C of flavivirus capsids, as well as the structure of histones dimers, domain-swapped transcription factors, and membrane-interacting BAK domains. The strong oligomerization properties of the isolated dArc lobe domains explain the ability of dArc to form capsids in the absence of any large N-terminal domain, in contrast to the mammalian protein.
format	article
author	Erik I Hallin Sigurbjörn Markússon Lev Böttger Andrew E Torda Clive R Bramham Petri Kursula
author_facet	Erik I Hallin Sigurbjörn Markússon Lev Böttger Andrew E Torda Clive R Bramham Petri Kursula
author_sort	Erik I Hallin
title	Crystal and solution structures reveal oligomerization of individual capsid homology domains of Drosophila Arc.
title_short	Crystal and solution structures reveal oligomerization of individual capsid homology domains of Drosophila Arc.
title_full	Crystal and solution structures reveal oligomerization of individual capsid homology domains of Drosophila Arc.
title_fullStr	Crystal and solution structures reveal oligomerization of individual capsid homology domains of Drosophila Arc.
title_full_unstemmed	Crystal and solution structures reveal oligomerization of individual capsid homology domains of Drosophila Arc.
title_sort	crystal and solution structures reveal oligomerization of individual capsid homology domains of drosophila arc.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/f34bcf4d31044cea8105ca392cd38f76
work_keys_str_mv	AT erikihallin crystalandsolutionstructuresrevealoligomerizationofindividualcapsidhomologydomainsofdrosophilaarc AT sigurbjornmarkusson crystalandsolutionstructuresrevealoligomerizationofindividualcapsidhomologydomainsofdrosophilaarc AT levbottger crystalandsolutionstructuresrevealoligomerizationofindividualcapsidhomologydomainsofdrosophilaarc AT andrewetorda crystalandsolutionstructuresrevealoligomerizationofindividualcapsidhomologydomainsofdrosophilaarc AT cliverbramham crystalandsolutionstructuresrevealoligomerizationofindividualcapsidhomologydomainsofdrosophilaarc AT petrikursula crystalandsolutionstructuresrevealoligomerizationofindividualcapsidhomologydomainsofdrosophilaarc
_version_	1718375638950215680

Crystal and solution structures reveal oligomerization of individual capsid homology domains of Drosophila Arc.

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