The Mimivirus L375 Nudix enzyme hydrolyzes the 5' mRNA cap.

The giant Mimivirus is a member of the nucleocytoplasmic large DNA viruses (NCLDV), a group of diverse viruses that contain double-stranded DNA (dsDNA) genomes that replicate primarily in eukaryotic hosts. Two members of the NCLDV, Vaccinia Virus (VACV) and African Swine Fever Virus (ASFV), both syn...

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Autores principales:	Grace Kago, Susan Parrish
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/d61737a1ded64edf8381858af0183e67
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spelling	oai:doaj.org-article:d61737a1ded64edf8381858af0183e672021-12-02T20:06:08ZThe Mimivirus L375 Nudix enzyme hydrolyzes the 5' mRNA cap.1932-620310.1371/journal.pone.0245820https://doaj.org/article/d61737a1ded64edf8381858af0183e672021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0245820https://doaj.org/toc/1932-6203The giant Mimivirus is a member of the nucleocytoplasmic large DNA viruses (NCLDV), a group of diverse viruses that contain double-stranded DNA (dsDNA) genomes that replicate primarily in eukaryotic hosts. Two members of the NCLDV, Vaccinia Virus (VACV) and African Swine Fever Virus (ASFV), both synthesize Nudix enzymes that have been shown to decap mRNA, a process thought to accelerate viral and host mRNA turnover and promote the shutoff of host protein synthesis. Mimivirus encodes two Nudix enzymes in its genome, denoted as L375 and L534. Importantly, L375 exhibits sequence similarity to ASFV-DP and eukaryotic Dcp2, two Nudix enzymes shown to possess mRNA decapping activity. In this work, we demonstrate that recombinant Mimivirus L375 cleaves the 5' m7GpppN mRNA cap, releasing m7GDP as a product. L375 did not significantly cleave mRNAs containing an unmethylated 5'GpppN cap, indicating that this enzyme specifically hydrolyzes methylated-capped transcripts. A point mutation in the L375 Nudix motif completely eliminated cap hydrolysis, showing that decapping activity is dependent on this motif. Addition of uncapped RNA significantly reduced L375 decapping activity, suggesting that L375 may recognize its substrate through interaction with the RNA body.Grace KagoSusan ParrishPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 9, p e0245820 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Grace Kago Susan Parrish The Mimivirus L375 Nudix enzyme hydrolyzes the 5' mRNA cap.
description	The giant Mimivirus is a member of the nucleocytoplasmic large DNA viruses (NCLDV), a group of diverse viruses that contain double-stranded DNA (dsDNA) genomes that replicate primarily in eukaryotic hosts. Two members of the NCLDV, Vaccinia Virus (VACV) and African Swine Fever Virus (ASFV), both synthesize Nudix enzymes that have been shown to decap mRNA, a process thought to accelerate viral and host mRNA turnover and promote the shutoff of host protein synthesis. Mimivirus encodes two Nudix enzymes in its genome, denoted as L375 and L534. Importantly, L375 exhibits sequence similarity to ASFV-DP and eukaryotic Dcp2, two Nudix enzymes shown to possess mRNA decapping activity. In this work, we demonstrate that recombinant Mimivirus L375 cleaves the 5' m7GpppN mRNA cap, releasing m7GDP as a product. L375 did not significantly cleave mRNAs containing an unmethylated 5'GpppN cap, indicating that this enzyme specifically hydrolyzes methylated-capped transcripts. A point mutation in the L375 Nudix motif completely eliminated cap hydrolysis, showing that decapping activity is dependent on this motif. Addition of uncapped RNA significantly reduced L375 decapping activity, suggesting that L375 may recognize its substrate through interaction with the RNA body.
format	article
author	Grace Kago Susan Parrish
author_facet	Grace Kago Susan Parrish
author_sort	Grace Kago
title	The Mimivirus L375 Nudix enzyme hydrolyzes the 5' mRNA cap.
title_short	The Mimivirus L375 Nudix enzyme hydrolyzes the 5' mRNA cap.
title_full	The Mimivirus L375 Nudix enzyme hydrolyzes the 5' mRNA cap.
title_fullStr	The Mimivirus L375 Nudix enzyme hydrolyzes the 5' mRNA cap.
title_full_unstemmed	The Mimivirus L375 Nudix enzyme hydrolyzes the 5' mRNA cap.
title_sort	mimivirus l375 nudix enzyme hydrolyzes the 5' mrna cap.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/d61737a1ded64edf8381858af0183e67
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The Mimivirus L375 Nudix enzyme hydrolyzes the 5' mRNA cap.

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