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Structural basis for retroviral integration into nucleosomes.

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Title: Structural basis for retroviral integration into nucleosomes.
Authors: Maskell, Daniel P., Renault, Ludovic, Serrao, Erik, Lesbats, Paul, Matadeen, Rishi, Hare, Stephen, Lindemann, Dirk, Engelman, Alan N., Costa, Alessandro, Cherepanov, Peter
Source: Nature. 7/16/2015, Vol. 523 Issue 7560, p366-369. 4p. 4 Diagrams, 1 Chart, 8 Graphs.
Subjects: Retroviruses, Chromatin, Integrases, Virus-induced enzymes, Foamy viruses, DNA
Abstract: Retroviral integration is catalysed by a tetramer of integrase (IN) assembled on viral DNA ends in a stable complex, known as the intasome. How the intasome interfaces with chromosomal DNA, which exists in the form of nucleosomal arrays, is currently unknown. Here we show that the prototype foamy virus (PFV) intasome is proficient at stable capture of nucleosomes as targets for integration. Single-particle cryo-electron microscopy reveals a multivalent intasome-nucleosome interface involving both gyres of nucleosomal DNA and one H2A-H2B heterodimer. While the histone octamer remains intact, the DNA is lifted from the surface of the H2A-H2B heterodimer to allow integration at strongly preferred superhelix location ±3.5 positions. Amino acid substitutions disrupting these contacts impinge on the ability of the intasome to engage nucleosomes in vitro and redistribute viral integration sites on the genomic scale. Our findings elucidate the molecular basis for nucleosome capture by the viral DNA recombination machinery and the underlying nucleosome plasticity that allows integration. [ABSTRACT FROM AUTHOR]
Copyright of Nature is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Psychology and Behavioral Sciences Collection
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  Data: Structural basis for retroviral integration into nucleosomes.
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  Data: <searchLink fieldCode="AR" term="%22Maskell%2C+Daniel+P%2E%22">Maskell, Daniel P.</searchLink><br /><searchLink fieldCode="AR" term="%22Renault%2C+Ludovic%22">Renault, Ludovic</searchLink><br /><searchLink fieldCode="AR" term="%22Serrao%2C+Erik%22">Serrao, Erik</searchLink><br /><searchLink fieldCode="AR" term="%22Lesbats%2C+Paul%22">Lesbats, Paul</searchLink><br /><searchLink fieldCode="AR" term="%22Matadeen%2C+Rishi%22">Matadeen, Rishi</searchLink><br /><searchLink fieldCode="AR" term="%22Hare%2C+Stephen%22">Hare, Stephen</searchLink><br /><searchLink fieldCode="AR" term="%22Lindemann%2C+Dirk%22">Lindemann, Dirk</searchLink><br /><searchLink fieldCode="AR" term="%22Engelman%2C+Alan+N%2E%22">Engelman, Alan N.</searchLink><br /><searchLink fieldCode="AR" term="%22Costa%2C+Alessandro%22">Costa, Alessandro</searchLink><br /><searchLink fieldCode="AR" term="%22Cherepanov%2C+Peter%22">Cherepanov, Peter</searchLink>
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  Data: <searchLink fieldCode="JN" term="%22Nature%22">Nature</searchLink>. 7/16/2015, Vol. 523 Issue 7560, p366-369. 4p. 4 Diagrams, 1 Chart, 8 Graphs.
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  Data: <searchLink fieldCode="DE" term="%22Retroviruses%22">Retroviruses</searchLink><br /><searchLink fieldCode="DE" term="%22Chromatin%22">Chromatin</searchLink><br /><searchLink fieldCode="DE" term="%22Integrases%22">Integrases</searchLink><br /><searchLink fieldCode="DE" term="%22Virus-induced+enzymes%22">Virus-induced enzymes</searchLink><br /><searchLink fieldCode="DE" term="%22Foamy+viruses%22">Foamy viruses</searchLink><br /><searchLink fieldCode="DE" term="%22DNA%22">DNA</searchLink>
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  Data: Retroviral integration is catalysed by a tetramer of integrase (IN) assembled on viral DNA ends in a stable complex, known as the intasome. How the intasome interfaces with chromosomal DNA, which exists in the form of nucleosomal arrays, is currently unknown. Here we show that the prototype foamy virus (PFV) intasome is proficient at stable capture of nucleosomes as targets for integration. Single-particle cryo-electron microscopy reveals a multivalent intasome-nucleosome interface involving both gyres of nucleosomal DNA and one H2A-H2B heterodimer. While the histone octamer remains intact, the DNA is lifted from the surface of the H2A-H2B heterodimer to allow integration at strongly preferred superhelix location ±3.5 positions. Amino acid substitutions disrupting these contacts impinge on the ability of the intasome to engage nucleosomes in vitro and redistribute viral integration sites on the genomic scale. Our findings elucidate the molecular basis for nucleosome capture by the viral DNA recombination machinery and the underlying nucleosome plasticity that allows integration. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Nature is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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