Mass spectrometric based detection of protein nucleotidylation in the RNA polymerase of SARS-CoV-2

Nidovirus RNA synthesis machineries catalyze nucleotide transfer, but characterization of this activity is limited using existing methods. Here the nucleotidyl transferase activity of SARSCoV-2 replicase proteins is characterized by mass spectrometry of GMP and UMP protein adducts, allowing identifi...

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Autores principales:	Brian J. Conti, Andrew S. Leicht, Robert N. Kirchdoerfer, Michael R. Sussman
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/1d91d20fca29400cb31f80048668475b
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spelling	oai:doaj.org-article:1d91d20fca29400cb31f80048668475b2021-12-02T17:05:48ZMass spectrometric based detection of protein nucleotidylation in the RNA polymerase of SARS-CoV-210.1038/s42004-021-00476-42399-3669https://doaj.org/article/1d91d20fca29400cb31f80048668475b2021-03-01T00:00:00Zhttps://doi.org/10.1038/s42004-021-00476-4https://doaj.org/toc/2399-3669Nidovirus RNA synthesis machineries catalyze nucleotide transfer, but characterization of this activity is limited using existing methods. Here the nucleotidyl transferase activity of SARSCoV-2 replicase proteins is characterized by mass spectrometry of GMP and UMP protein adducts, allowing identification of nucleotidylation sites in vitro.Brian J. ContiAndrew S. LeichtRobert N. KirchdoerferMichael R. SussmanNature PortfolioarticleChemistryQD1-999ENCommunications Chemistry, Vol 4, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Chemistry QD1-999
spellingShingle	Chemistry QD1-999 Brian J. Conti Andrew S. Leicht Robert N. Kirchdoerfer Michael R. Sussman Mass spectrometric based detection of protein nucleotidylation in the RNA polymerase of SARS-CoV-2
description	Nidovirus RNA synthesis machineries catalyze nucleotide transfer, but characterization of this activity is limited using existing methods. Here the nucleotidyl transferase activity of SARSCoV-2 replicase proteins is characterized by mass spectrometry of GMP and UMP protein adducts, allowing identification of nucleotidylation sites in vitro.
format	article
author	Brian J. Conti Andrew S. Leicht Robert N. Kirchdoerfer Michael R. Sussman
author_facet	Brian J. Conti Andrew S. Leicht Robert N. Kirchdoerfer Michael R. Sussman
author_sort	Brian J. Conti
title	Mass spectrometric based detection of protein nucleotidylation in the RNA polymerase of SARS-CoV-2
title_short	Mass spectrometric based detection of protein nucleotidylation in the RNA polymerase of SARS-CoV-2
title_full	Mass spectrometric based detection of protein nucleotidylation in the RNA polymerase of SARS-CoV-2
title_fullStr	Mass spectrometric based detection of protein nucleotidylation in the RNA polymerase of SARS-CoV-2
title_full_unstemmed	Mass spectrometric based detection of protein nucleotidylation in the RNA polymerase of SARS-CoV-2
title_sort	mass spectrometric based detection of protein nucleotidylation in the rna polymerase of sars-cov-2
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/1d91d20fca29400cb31f80048668475b
work_keys_str_mv	AT brianjconti massspectrometricbaseddetectionofproteinnucleotidylationinthernapolymeraseofsarscov2 AT andrewsleicht massspectrometricbaseddetectionofproteinnucleotidylationinthernapolymeraseofsarscov2 AT robertnkirchdoerfer massspectrometricbaseddetectionofproteinnucleotidylationinthernapolymeraseofsarscov2 AT michaelrsussman massspectrometricbaseddetectionofproteinnucleotidylationinthernapolymeraseofsarscov2
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Mass spectrometric based detection of protein nucleotidylation in the RNA polymerase of SARS-CoV-2

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