A Heat Shock Protein 48 (HSP48) Biomolecular Condensate Is Induced during <named-content content-type="genus-species">Dictyostelium discoideum</named-content> Development

ABSTRACT The social amoeba Dictyostelium discoideum’s proteome contains a vast array of simple sequence repeats, providing a unique model to investigate proteostasis. Upon conditions of cellular stress, D. discoideum undergoes a developmental process, transitioning from a unicellular amoeba to a mul...

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Autores principales:	Stephanie Santarriaga, Alicia Fikejs, Jamie Scaglione, K. Matthew Scaglione
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2019
Materias:	Dictyostelium discoideum chaperone phase separation small heat shock protein Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/a268bffb7a28466b97980479c8970da0
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spelling	oai:doaj.org-article:a268bffb7a28466b97980479c8970da02021-11-15T15:22:20ZA Heat Shock Protein 48 (HSP48) Biomolecular Condensate Is Induced during <named-content content-type="genus-species">Dictyostelium discoideum</named-content> Development10.1128/mSphere.00314-192379-5042https://doaj.org/article/a268bffb7a28466b97980479c8970da02019-06-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mSphere.00314-19https://doaj.org/toc/2379-5042ABSTRACT The social amoeba Dictyostelium discoideum’s proteome contains a vast array of simple sequence repeats, providing a unique model to investigate proteostasis. Upon conditions of cellular stress, D. discoideum undergoes a developmental process, transitioning from a unicellular amoeba to a multicellular fruiting body. Little is known about how proteostasis is maintained during D. discoideum’s developmental process. Here, we have identified a novel α-crystallin domain-containing protein, heat shock protein 48 (HSP48), that is upregulated during D. discoideum development. HSP48 functions in part by forming a biomolecular condensate via its highly positively charged intrinsically disordered carboxy terminus. In addition to HSP48, the highly negatively charged primordial chaperone polyphosphate is also upregulated during D. discoideum development, and polyphosphate functions to stabilize HSP48. Upon germination, levels of both HSP48 and polyphosphate dramatically decrease, consistent with a role for HSP48 and polyphosphate during development. Together, our data demonstrate that HSP48 is strongly induced during Dictyostelium discoideum development. We also demonstrate that HSP48 forms a biomolecular condensate and that polyphosphate is necessary to stabilize the HSP48 biomolecular condensate. IMPORTANCE During cellular stress, many microbes undergo a transition to a dormant state. This includes the social amoeba Dictyostelium discoideum that transitions from a unicellular amoeba to a multicellular fruiting body upon starvation. In this work, we identify heat shock protein 48 (HSP48) as a chaperone that is induced during development. We also show that HSP48 forms a biomolecular condensate and is stabilized by polyphosphate. The findings here identify Dictyostelium discoideum as a novel microbe to investigate protein quality control pathways during the transition to dormancy.Stephanie SantarriagaAlicia FikejsJamie ScaglioneK. Matthew ScaglioneAmerican Society for MicrobiologyarticleDictyostelium discoideumchaperonephase separationsmall heat shock proteinMicrobiologyQR1-502ENmSphere, Vol 4, Iss 3 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Dictyostelium discoideum chaperone phase separation small heat shock protein Microbiology QR1-502
spellingShingle	Dictyostelium discoideum chaperone phase separation small heat shock protein Microbiology QR1-502 Stephanie Santarriaga Alicia Fikejs Jamie Scaglione K. Matthew Scaglione A Heat Shock Protein 48 (HSP48) Biomolecular Condensate Is Induced during <named-content content-type="genus-species">Dictyostelium discoideum</named-content> Development
description	ABSTRACT The social amoeba Dictyostelium discoideum’s proteome contains a vast array of simple sequence repeats, providing a unique model to investigate proteostasis. Upon conditions of cellular stress, D. discoideum undergoes a developmental process, transitioning from a unicellular amoeba to a multicellular fruiting body. Little is known about how proteostasis is maintained during D. discoideum’s developmental process. Here, we have identified a novel α-crystallin domain-containing protein, heat shock protein 48 (HSP48), that is upregulated during D. discoideum development. HSP48 functions in part by forming a biomolecular condensate via its highly positively charged intrinsically disordered carboxy terminus. In addition to HSP48, the highly negatively charged primordial chaperone polyphosphate is also upregulated during D. discoideum development, and polyphosphate functions to stabilize HSP48. Upon germination, levels of both HSP48 and polyphosphate dramatically decrease, consistent with a role for HSP48 and polyphosphate during development. Together, our data demonstrate that HSP48 is strongly induced during Dictyostelium discoideum development. We also demonstrate that HSP48 forms a biomolecular condensate and that polyphosphate is necessary to stabilize the HSP48 biomolecular condensate. IMPORTANCE During cellular stress, many microbes undergo a transition to a dormant state. This includes the social amoeba Dictyostelium discoideum that transitions from a unicellular amoeba to a multicellular fruiting body upon starvation. In this work, we identify heat shock protein 48 (HSP48) as a chaperone that is induced during development. We also show that HSP48 forms a biomolecular condensate and is stabilized by polyphosphate. The findings here identify Dictyostelium discoideum as a novel microbe to investigate protein quality control pathways during the transition to dormancy.
format	article
author	Stephanie Santarriaga Alicia Fikejs Jamie Scaglione K. Matthew Scaglione
author_facet	Stephanie Santarriaga Alicia Fikejs Jamie Scaglione K. Matthew Scaglione
author_sort	Stephanie Santarriaga
title	A Heat Shock Protein 48 (HSP48) Biomolecular Condensate Is Induced during <named-content content-type="genus-species">Dictyostelium discoideum</named-content> Development
title_short	A Heat Shock Protein 48 (HSP48) Biomolecular Condensate Is Induced during <named-content content-type="genus-species">Dictyostelium discoideum</named-content> Development
title_full	A Heat Shock Protein 48 (HSP48) Biomolecular Condensate Is Induced during <named-content content-type="genus-species">Dictyostelium discoideum</named-content> Development
title_fullStr	A Heat Shock Protein 48 (HSP48) Biomolecular Condensate Is Induced during <named-content content-type="genus-species">Dictyostelium discoideum</named-content> Development
title_full_unstemmed	A Heat Shock Protein 48 (HSP48) Biomolecular Condensate Is Induced during <named-content content-type="genus-species">Dictyostelium discoideum</named-content> Development
title_sort	heat shock protein 48 (hsp48) biomolecular condensate is induced during <named-content content-type="genus-species">dictyostelium discoideum</named-content> development
publisher	American Society for Microbiology
publishDate	2019
url	https://doaj.org/article/a268bffb7a28466b97980479c8970da0
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A Heat Shock Protein 48 (HSP48) Biomolecular Condensate Is Induced during <named-content content-type="genus-species">Dictyostelium discoideum</named-content> Development

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