MersV1, Istex, Corpus, bibRecord, 001F71

Interactions between HIV-1 nucleocapsid protein and viral DNA may have important functions in the viral life cycle

Identifieur interne : 001F71 ( Istex/Corpus ); précédent : 001F70; suivant : 001F72

Interactions between HIV-1 nucleocapsid protein and viral DNA may have important functions in the viral life cycle

Auteurs : Mary Lapadat-Tapolsky ; Hugues De Rocquigny ; Dik Van Gent ; Bernard Roques ; Ronald Plasterk ; Jean-Luc Darlix

Source :

Nucleic Acids Research [ 0305-1048 ] ; 1993.

RBID : ISTEX:476B9B81B575F1EBB88814408515849DD7F0B261

Abstract

In the virion core of retroviruses, the genomic RNA is tightly associated with nucleocapsid (NC) protein molecules, forming the nucleocapsid structure. NC protein, a highly basic protein with two zinc fingers, is indispensable for RNA dimerization, encapsidation and the Initiation of reverse transcription in avian, murine and human retroviruses. Here we show that NC protein of HIV-1 (NCp7) and NCp7 mutants bind to DNA fragments representing proviral DNA sequences, forming stable complexes. NCp7 and NCp7 mutants form high molecular weight complexes with large DNA fragments and show cooperativity in binding to the DNAs. It appears that the conserved basic residues, and not the zinc fingers, are important for complex formation. In addition, NCp7 and several NCp7 mutants protect DNAs from nuclease digestion while the DNA ends appear to be poorly protected. NCp7 has been found to bind to strong stop cDNA, the initial product of reverse transcription, and to promote the annealing of this cDNA to HIV-1 RNA corresponding to the 3′ end of the genome. In addition, NCp7 slightly stimulates an in vitro IN cleavage assay. These results indicate that the interactions between NCp7 and proviral DNA may be important during provirus synthesis and/or prior to integration.

Url:

https://api.istex.fr/ark:/67375/HXZ-MP90X82X-S/fulltext.pdf

DOI: 10.1093/nar/21.4.831

Links to Exploration step

ISTEX:476B9B81B575F1EBB88814408515849DD7F0B261

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<profileDesc><abstract><p>In the virion core of retroviruses, the genomic RNA is tightly associated with nucleocapsid (NC) protein molecules, forming the nucleocapsid structure. NC protein, a highly basic protein with two zinc fingers, is indispensable for RNA dimerization, encapsidation and the Initiation of reverse transcription in avian, murine and human retroviruses. Here we show that NC protein of HIV-1 (NCp7) and NCp7 mutants bind to DNA fragments representing proviral DNA sequences, forming stable complexes. NCp7 and NCp7 mutants form high molecular weight complexes with large DNA fragments and show cooperativity in binding to the DNAs. It appears that the conserved basic residues, and not the zinc fingers, are important for complex formation. In addition, NCp7 and several NCp7 mutants protect DNAs from nuclease digestion while the DNA ends appear to be poorly protected. NCp7 has been found to bind to strong stop cDNA, the initial product of reverse transcription, and to promote the annealing of this cDNA to HIV-1 RNA corresponding to the 3′ end of the genome. In addition, NCp7 slightly stimulates an <hi rend="italic">in vitro</hi>
 IN cleavage assay. These results indicate that the interactions between NCp7 and proviral DNA may be important during provirus synthesis and/or prior to integration.</p>
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<journal-title>Nucleic Acids Research</journal-title>

<issn pub-type="epub">1362-4962</issn>

<issn pub-type="ppub">0305-1048</issn>

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<article-title>Interactions between HIV-1 nucleocapsid protein and viral DNA may have important functions in the viral life cycle</article-title>

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<name><surname>Lapadat-Tapolsky</surname>
<given-names>Mary</given-names>
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<name><surname>Rocquigny</surname>
<given-names>Hugues De</given-names>
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<xref ref-type="aff" rid="au1"><sup>1</sup>
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<name><surname>Gent</surname>
<given-names>Dik Van</given-names>
</name>
<xref ref-type="aff" rid="au2"><sup>2</sup>
</xref>

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<contrib contrib-type="author">

<name><surname>Roques</surname>
<given-names>Bernard</given-names>
</name>
<xref ref-type="aff" rid="au1"><sup>1</sup>
</xref>

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<name><surname>Plasterk</surname>
<given-names>Ronald</given-names>
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<xref ref-type="aff" rid="au2"><sup>2</sup>
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<name><surname>Darlix</surname>
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<aff id="au2"><sup>2</sup>
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<year>1992</year>

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<year>1993</year>

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<p>In the virion core of retroviruses, the genomic RNA is tightly associated with nucleocapsid (NC) protein molecules, forming the nucleocapsid structure. NC protein, a highly basic protein with two zinc fingers, is indispensable for RNA dimerization, encapsidation and the Initiation of reverse transcription in avian, murine and human retroviruses. Here we show that NC protein of HIV-1 (NCp7) and NCp7 mutants bind to DNA fragments representing proviral DNA sequences, forming stable complexes. NCp7 and NCp7 mutants form high molecular weight complexes with large DNA fragments and show cooperativity in binding to the DNAs. It appears that the conserved basic residues, and not the zinc fingers, are important for complex formation. In addition, NCp7 and several NCp7 mutants protect DNAs from nuclease digestion while the DNA ends appear to be poorly protected. NCp7 has been found to bind to strong stop cDNA, the initial product of reverse transcription, and to promote the annealing of this cDNA to HIV-1 RNA corresponding to the 3′ end of the genome. In addition, NCp7 slightly stimulates an <italic>in vitro</italic>
 IN cleavage assay. These results indicate that the interactions between NCp7 and proviral DNA may be important during provirus synthesis and/or prior to integration.</p>

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Interactions between HIV-1 nucleocapsid protein and viral DNA may have important functions in the viral life cycle

Interactions between HIV-1 nucleocapsid protein and viral DNA may have important functions in the viral life cycle

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