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1H, 13C, and 15N backbone chemical shift assignments of coronavirus-2 non-structural protein Nsp10

Kubatova, N. and Qureshi, N. S. and Altincekic, N. and Abele, R. and Bains, J. K. and Ceylan, B. and Ferner, J. and Fuks, C. and Hargittay, B. and Hutchison, M. T. and de Jesus, V. and Kutz, F. and Wirtz Martin, M. A. and Meiser, N. and Linhard, V. and Pyper, D. J. and Trucks, S. and Fürtig, B. and Hengesbach, M. and Löhr, F. and Richter, C and Saxena, K. and Schlundt, A. and Schwalbe, H. and Sreeramulu, S. and Wacker, A. and Weigand, Julia E. and Wirmer-Bartoschek, J. and Wöhnert, J. (2020):
1H, 13C, and 15N backbone chemical shift assignments of coronavirus-2 non-structural protein Nsp10.
In: Biomolecular NMR assignments, 2020, Springer, ISSN 1874-270X,
DOI: 10.1007/s12104-020-09984-1,
[Article]

Abstract

The international Covid19-NMR consortium aims at the comprehensive spectroscopic characterization of SARS-CoV-2 RNA elements and proteins and will provide NMR chemical shift assignments of the molecular components of this virus. The SARS-CoV-2 genome encodes approximately 30 different proteins. Four of these proteins are involved in forming the viral envelope or in the packaging of the RNA genome and are therefore called structural proteins. The other proteins fulfill a variety of functions during the viral life cycle and comprise the so-called non-structural proteins (nsps). Here, we report the near-complete NMR resonance assignment for the backbone chemical shifts of the non-structural protein 10 (nsp10). Nsp10 is part of the viral replication-transcription complex (RTC). It aids in synthesizing and modifying the genomic and subgenomic RNAs. Via its interaction with nsp14, it ensures transcriptional fidelity of the RNA-dependent RNA polymerase, and through its stimulation of the methyltransferase activity of nsp16, it aids in synthesizing the RNA cap structures which protect the viral RNAs from being recognized by the innate immune system. Both of these functions can be potentially targeted by drugs. Our data will aid in performing additional NMR-based characterizations, and provide a basis for the identification of possible small molecule ligands interfering with nsp10 exerting its essential role in viral replication.

Item Type: Article
Erschienen: 2020
Creators: Kubatova, N. and Qureshi, N. S. and Altincekic, N. and Abele, R. and Bains, J. K. and Ceylan, B. and Ferner, J. and Fuks, C. and Hargittay, B. and Hutchison, M. T. and de Jesus, V. and Kutz, F. and Wirtz Martin, M. A. and Meiser, N. and Linhard, V. and Pyper, D. J. and Trucks, S. and Fürtig, B. and Hengesbach, M. and Löhr, F. and Richter, C and Saxena, K. and Schlundt, A. and Schwalbe, H. and Sreeramulu, S. and Wacker, A. and Weigand, Julia E. and Wirmer-Bartoschek, J. and Wöhnert, J.
Title: 1H, 13C, and 15N backbone chemical shift assignments of coronavirus-2 non-structural protein Nsp10
Language: English
Abstract:

The international Covid19-NMR consortium aims at the comprehensive spectroscopic characterization of SARS-CoV-2 RNA elements and proteins and will provide NMR chemical shift assignments of the molecular components of this virus. The SARS-CoV-2 genome encodes approximately 30 different proteins. Four of these proteins are involved in forming the viral envelope or in the packaging of the RNA genome and are therefore called structural proteins. The other proteins fulfill a variety of functions during the viral life cycle and comprise the so-called non-structural proteins (nsps). Here, we report the near-complete NMR resonance assignment for the backbone chemical shifts of the non-structural protein 10 (nsp10). Nsp10 is part of the viral replication-transcription complex (RTC). It aids in synthesizing and modifying the genomic and subgenomic RNAs. Via its interaction with nsp14, it ensures transcriptional fidelity of the RNA-dependent RNA polymerase, and through its stimulation of the methyltransferase activity of nsp16, it aids in synthesizing the RNA cap structures which protect the viral RNAs from being recognized by the innate immune system. Both of these functions can be potentially targeted by drugs. Our data will aid in performing additional NMR-based characterizations, and provide a basis for the identification of possible small molecule ligands interfering with nsp10 exerting its essential role in viral replication.

Journal or Publication Title: Biomolecular NMR assignments
Journal volume: 2020
Publisher: Springer
Divisions: 10 Department of Biology
10 Department of Biology > RNA Biochemistry
Date Deposited: 05 Mar 2021 08:33
DOI: 10.1007/s12104-020-09984-1
Official URL: https://link.springer.com/article/10.1007/s12104-020-09984-1...
Identification Number: pmid:33159807
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