Cellular mRNA export factor UAP56 recognizes nucleic acid binding site of influenza virus NP protein.


Journal

Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516

Informations de publication

Date de publication:
30 04 2020
Historique:
received: 03 01 2020
accepted: 09 02 2020
pubmed: 23 2 2020
medline: 11 11 2020
entrez: 23 2 2020
Statut: ppublish

Résumé

Influenza A virus nucleoprotein (NP) is a structural component that encapsulates the viral genome into the form of ribonucleoprotein complexes (vRNPs). Efficient assembly of vRNPs is critical for the virus life cycle. The assembly route from RNA-free NP to the NP-RNA polymer in vRNPs has been suggested to require a cellular factor UAP56, but the mechanism is poorly understood. Here, we characterized the interaction between NP and UAP56 using recombinant proteins and showed that UAP56 features two NP binding sites. In addition to the UAP56 core comprised of two RecA domains, we identified the N-terminal extension (NTE) of UAP56 as a previously unknown NP binding site. In particular, UAP56-NTE recognizes the nucleic acid binding region of NP. This corroborates our observation that binding of UAP56-NTE and RNA to NP is mutually exclusive. Collectively, our results reveal the molecular basis for how UAP56 acts on RNA-free NP, and provide new insights into NP-mediated influenza genome packaging.

Identifiants

pubmed: 32085897
pii: S0006-291X(20)30327-2
doi: 10.1016/j.bbrc.2020.02.059
pmc: PMC7132624
mid: NIHMS1564198
pii:
doi:

Substances chimiques

NP protein, Influenza A virus 0
Nucleocapsid Proteins 0
RNA, Messenger 0
RNA-Binding Proteins 0
Ribonucleoproteins 0
Viral Core Proteins 0
DDX39B protein, human EC 3.6.1.-
DEAD-box RNA Helicases EC 3.6.4.13

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

259-264

Subventions

Organisme : NIGMS NIH HHS
ID : R35 GM133743
Pays : United States

Informations de copyright

Copyright © 2020 Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interests The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

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Auteurs

Andrew K Morris (AK)

Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA.

Zhen Wang (Z)

Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA; Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA.

Austin L Ivey (AL)

Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA.

Yihu Xie (Y)

Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA.

Pate S Hill (PS)

Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA.

Kevin L Schey (KL)

Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA; Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA.

Yi Ren (Y)

Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA. Electronic address: yi.ren@vanderbilt.edu.

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Classifications MeSH