Prokaryotic Argonaute from Archaeoglobus fulgidus interacts with DNA as a homodimer

Abstract Argonaute (Ago) proteins are found in all three domains of life. The best-characterized group is eukaryotic Argonautes (eAgos), which are the core of RNA interference. The best understood prokaryotic Ago (pAgo) proteins are full-length pAgos. They are composed of four major structural/funct...

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Autores principales:	Edvardas Golovinas, Danielis Rutkauskas, Elena Manakova, Marija Jankunec, Arunas Silanskas, Giedrius Sasnauskas, Mindaugas Zaremba
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/39d5feff9959403aac935edc12e7bc4d
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spelling	oai:doaj.org-article:39d5feff9959403aac935edc12e7bc4d2021-12-02T13:19:28ZProkaryotic Argonaute from Archaeoglobus fulgidus interacts with DNA as a homodimer10.1038/s41598-021-83889-42045-2322https://doaj.org/article/39d5feff9959403aac935edc12e7bc4d2021-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-83889-4https://doaj.org/toc/2045-2322Abstract Argonaute (Ago) proteins are found in all three domains of life. The best-characterized group is eukaryotic Argonautes (eAgos), which are the core of RNA interference. The best understood prokaryotic Ago (pAgo) proteins are full-length pAgos. They are composed of four major structural/functional domains (N, PAZ, MID, and PIWI) and thereby closely resemble eAgos. It was demonstrated that full-length pAgos function as prokaryotic antiviral systems, with the PIWI domain performing cleavage of invading nucleic acids. However, the majority of identified pAgos are shorter and catalytically inactive (encode just MID and inactive PIWI domains), thus their action mechanism and function remain unknown. In this work we focus on AfAgo, a short pAgo protein encoded by an archaeon Archaeoglobus fulgidus. We find that in all previously solved AfAgo structures, its two monomers form substantial dimerization interfaces involving the C-terminal β-sheets. Led by this finding, we have employed various biochemical and biophysical assays, including SEC-MALS, SAXS, single-molecule FRET, and AFM, to show that AfAgo is indeed a homodimer in solution, which is capable of simultaneous interaction with two DNA molecules. This finding underscores the diversity of prokaryotic Agos and broadens the range of currently known Argonaute-nucleic acid interaction mechanisms.Edvardas GolovinasDanielis RutkauskasElena ManakovaMarija JankunecArunas SilanskasGiedrius SasnauskasMindaugas ZarembaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Edvardas Golovinas Danielis Rutkauskas Elena Manakova Marija Jankunec Arunas Silanskas Giedrius Sasnauskas Mindaugas Zaremba Prokaryotic Argonaute from Archaeoglobus fulgidus interacts with DNA as a homodimer
description	Abstract Argonaute (Ago) proteins are found in all three domains of life. The best-characterized group is eukaryotic Argonautes (eAgos), which are the core of RNA interference. The best understood prokaryotic Ago (pAgo) proteins are full-length pAgos. They are composed of four major structural/functional domains (N, PAZ, MID, and PIWI) and thereby closely resemble eAgos. It was demonstrated that full-length pAgos function as prokaryotic antiviral systems, with the PIWI domain performing cleavage of invading nucleic acids. However, the majority of identified pAgos are shorter and catalytically inactive (encode just MID and inactive PIWI domains), thus their action mechanism and function remain unknown. In this work we focus on AfAgo, a short pAgo protein encoded by an archaeon Archaeoglobus fulgidus. We find that in all previously solved AfAgo structures, its two monomers form substantial dimerization interfaces involving the C-terminal β-sheets. Led by this finding, we have employed various biochemical and biophysical assays, including SEC-MALS, SAXS, single-molecule FRET, and AFM, to show that AfAgo is indeed a homodimer in solution, which is capable of simultaneous interaction with two DNA molecules. This finding underscores the diversity of prokaryotic Agos and broadens the range of currently known Argonaute-nucleic acid interaction mechanisms.
format	article
author	Edvardas Golovinas Danielis Rutkauskas Elena Manakova Marija Jankunec Arunas Silanskas Giedrius Sasnauskas Mindaugas Zaremba
author_facet	Edvardas Golovinas Danielis Rutkauskas Elena Manakova Marija Jankunec Arunas Silanskas Giedrius Sasnauskas Mindaugas Zaremba
author_sort	Edvardas Golovinas
title	Prokaryotic Argonaute from Archaeoglobus fulgidus interacts with DNA as a homodimer
title_short	Prokaryotic Argonaute from Archaeoglobus fulgidus interacts with DNA as a homodimer
title_full	Prokaryotic Argonaute from Archaeoglobus fulgidus interacts with DNA as a homodimer
title_fullStr	Prokaryotic Argonaute from Archaeoglobus fulgidus interacts with DNA as a homodimer
title_full_unstemmed	Prokaryotic Argonaute from Archaeoglobus fulgidus interacts with DNA as a homodimer
title_sort	prokaryotic argonaute from archaeoglobus fulgidus interacts with dna as a homodimer
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/39d5feff9959403aac935edc12e7bc4d
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Prokaryotic Argonaute from Archaeoglobus fulgidus interacts with DNA as a homodimer

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