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  1. Article ; Online: 1

    de Luna Marques, Aline / Caruso, Icaro Putinhon / Santana-Silva, Marcos Caique / Bezerra, Peter Reis / Araujo, Gabriela Rocha / Almeida, Fabio Ceneviva Lacerda / Amorim, Gisele Cardoso

    Biomolecular NMR assignments

    2021  Volume 15, Issue 1, Page(s) 153–157

    Abstract: Coronaviruses have become of great medical and scientific interest because of the Covid-19 pandemic. The hCoV-HKU1 is an endemic betacoronavirus that causes mild respiratory symptoms, although the infection can progress to severe lung disease and death. ... ...

    Abstract Coronaviruses have become of great medical and scientific interest because of the Covid-19 pandemic. The hCoV-HKU1 is an endemic betacoronavirus that causes mild respiratory symptoms, although the infection can progress to severe lung disease and death. During viral replication, a discontinuous transcription of the genome takes place, producing the subgenomic messenger RNAs. The nucleocapsid protein (N) plays a pivotal role in the regulation of this process, acting as an RNA chaperone and participating in the nucleocapsid assembly. The isolated N-terminal domain of protein N (N-NTD) specifically binds to the transcriptional regulatory sequences and control the melting of the double-stranded RNA. Here, we report the resonance assignments of the N-NTD of HKU1-CoV.
    MeSH term(s) Betacoronavirus/chemistry ; Carbon Isotopes ; Coronavirus Nucleocapsid Proteins/chemistry ; Escherichia coli/metabolism ; Hydrogen ; Magnetic Resonance Spectroscopy ; Nitrogen Isotopes ; Protein Binding ; Protein Domains ; Protein Structure, Secondary ; Software
    Chemical Substances Carbon Isotopes ; Coronavirus Nucleocapsid Proteins ; Nitrogen Isotopes ; Nitrogen-15 ; Hydrogen (7YNJ3PO35Z) ; Carbon-13 (FDJ0A8596D)
    Language English
    Publishing date 2021-01-03
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2388861-1
    ISSN 1874-270X ; 1874-2718
    ISSN (online) 1874-270X
    ISSN 1874-2718
    DOI 10.1007/s12104-020-09998-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Insights into the specificity for the interaction of the promiscuous SARS-CoV-2 nucleocapsid protein N-terminal domain with deoxyribonucleic acids

    Caruso, Icaro Putinhon / dos Santos Almeida, Vitor / do Amaral, Mariana Juliani / de Andrade, Guilherme Caldas / de Araújo, Gabriela Rocha / de Araújo, Talita Stelling / de Azevedo, Jéssica Moreira / Barbosa, Glauce Moreno / Bartkevihi, Leonardo / Bezerra, Peter Reis / dos Santos Cabral, Katia Maria / de Lourenço, Isabella Otênio / Malizia-Motta, Clara L.F. / de Luna Marques, Aline / Mebus-Antunes, Nathane Cunha / Neves-Martins, Thais Cristtina / de Sá, Jéssica Maróstica / Sanches, Karoline / Santana-Silva, Marcos Caique /
    Vasconcelos, Ariana Azevedo / da Silva Almeida, Marcius / de Amorim, Gisele Cardoso / Anobom, Cristiane Dinis / Da Poian, Andrea T. / Gomes-Neto, Francisco / Pinheiro, Anderson S. / Almeida, Fabio C.L.

    International journal of biological macromolecules. 2022 Apr. 01, v. 203

    2022  

    Abstract: The SARS-CoV-2 nucleocapsid protein (N) is a multifunctional promiscuous nucleic acid-binding protein, which plays a major role in nucleocapsid assembly and discontinuous RNA transcription, facilitating the template switch of transcriptional regulatory ... ...

    Abstract The SARS-CoV-2 nucleocapsid protein (N) is a multifunctional promiscuous nucleic acid-binding protein, which plays a major role in nucleocapsid assembly and discontinuous RNA transcription, facilitating the template switch of transcriptional regulatory sequences (TRS). Here, we dissect the structural features of the N protein N-terminal domain (N-NTD) and N-NTD plus the SR-rich motif (N-NTD-SR) upon binding to single and double-stranded TRS DNA, as well as their activities for dsTRS melting and TRS-induced liquid-liquid phase separation (LLPS). Our study gives insights on the specificity for N-NTD(-SR) interaction with TRS. We observed an approximation of the triple-thymidine (TTT) motif of the TRS to β-sheet II, giving rise to an orientation difference of ~25° between dsTRS and non-specific sequence (dsNS). It led to a local unfavorable energetic contribution that might trigger the melting activity. The thermodynamic parameters of binding of ssTRSs and dsTRS suggested that the duplex dissociation of the dsTRS in the binding cleft is entropically favorable. We showed a preference for TRS in the formation of liquid condensates when compared to NS. Moreover, our results on DNA binding may serve as a starting point for the design of inhibitors, including aptamers, against N, a possible therapeutic target essential for the virus infectivity.
    Keywords DNA ; RNA ; Severe acute respiratory syndrome coronavirus 2 ; dissociation ; liquids ; nucleocapsid ; nucleocapsid proteins ; oligonucleotides ; pathogenicity ; separation ; therapeutics ; thermodynamics ; transcription (genetics) ; viruses
    Language English
    Dates of publication 2022-0401
    Size p. 466-480.
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2022.01.121
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Cologne/Königswinter

    Zs.B 2374: Show issues Location:
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    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  3. Article ; Online: Insights into the specificity for the interaction of the promiscuous SARS-CoV-2 nucleocapsid protein N-terminal domain with deoxyribonucleic acids.

    Caruso, Icaro Putinhon / Dos Santos Almeida, Vitor / do Amaral, Mariana Juliani / de Andrade, Guilherme Caldas / de Araújo, Gabriela Rocha / de Araújo, Talita Stelling / de Azevedo, Jéssica Moreira / Barbosa, Glauce Moreno / Bartkevihi, Leonardo / Bezerra, Peter Reis / Dos Santos Cabral, Katia Maria / de Lourenço, Isabella Otênio / Malizia-Motta, Clara L F / de Luna Marques, Aline / Mebus-Antunes, Nathane Cunha / Neves-Martins, Thais Cristtina / de Sá, Jéssica Maróstica / Sanches, Karoline / Santana-Silva, Marcos Caique /
    Vasconcelos, Ariana Azevedo / da Silva Almeida, Marcius / de Amorim, Gisele Cardoso / Anobom, Cristiane Dinis / Da Poian, Andrea T / Gomes-Neto, Francisco / Pinheiro, Anderson S / Almeida, Fabio C L

    International journal of biological macromolecules

    2022  Volume 203, Page(s) 466–480

    Abstract: The SARS-CoV-2 nucleocapsid protein (N) is a multifunctional promiscuous nucleic acid-binding protein, which plays a major role in nucleocapsid assembly and discontinuous RNA transcription, facilitating the template switch of transcriptional regulatory ... ...

    Abstract The SARS-CoV-2 nucleocapsid protein (N) is a multifunctional promiscuous nucleic acid-binding protein, which plays a major role in nucleocapsid assembly and discontinuous RNA transcription, facilitating the template switch of transcriptional regulatory sequences (TRS). Here, we dissect the structural features of the N protein N-terminal domain (N-NTD) and N-NTD plus the SR-rich motif (N-NTD-SR) upon binding to single and double-stranded TRS DNA, as well as their activities for dsTRS melting and TRS-induced liquid-liquid phase separation (LLPS). Our study gives insights on the specificity for N-NTD(-SR) interaction with TRS. We observed an approximation of the triple-thymidine (TTT) motif of the TRS to β-sheet II, giving rise to an orientation difference of ~25° between dsTRS and non-specific sequence (dsNS). It led to a local unfavorable energetic contribution that might trigger the melting activity. The thermodynamic parameters of binding of ssTRSs and dsTRS suggested that the duplex dissociation of the dsTRS in the binding cleft is entropically favorable. We showed a preference for TRS in the formation of liquid condensates when compared to NS. Moreover, our results on DNA binding may serve as a starting point for the design of inhibitors, including aptamers, against N, a possible therapeutic target essential for the virus infectivity.
    MeSH term(s) Binding Sites ; COVID-19/virology ; DNA/chemistry ; DNA/metabolism ; Gene Expression Regulation, Viral ; Host-Pathogen Interactions ; Humans ; Hydrogen Bonding ; Models, Molecular ; Nucleic Acids/chemistry ; Nucleic Acids/metabolism ; Nucleocapsid Proteins/chemistry ; Nucleocapsid Proteins/metabolism ; Protein Binding ; Protein Interaction Domains and Motifs ; RNA/chemistry ; RNA/metabolism ; SARS-CoV-2/physiology ; Spectrum Analysis ; Structure-Activity Relationship
    Chemical Substances Nucleic Acids ; Nucleocapsid Proteins ; RNA (63231-63-0) ; DNA (9007-49-2)
    Language English
    Publishing date 2022-01-22
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2022.01.121
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.B 2374: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

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