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Virology

Hitching a lift on a histone

Nature Reviews Microbiology volume 4, pages 240–241 (2006)Cite this article

The team used affinity purification and mass spectrometry to look for potential protein binding partners for LANA. Among the proteins they identified were the core histones, H2A, H2B, H3 and H4. However, they also pulled out the proteins Ku70, Ku80 and PARP1 (polyadenosine diphosphate-ribose polymerase 1). By using mouse cells that were null or deficient for each of these latter three, the team observed that LANA's association with chromosomes was unperturbed. Therefore, by a process of elimination, the core histones were left as prime suspect.

In further immunoprecipitation experiments, the team showed that LANA specifically bound to histones H2A and H2B rather than H3 and H4. They then went on to prove that this specific interaction was necessary for chromosome association by showing that, in Xenopus sperm cells which lack H2A and H2B, LANA was dissociated from chromatin and that, by adding H2A and H2B to the system, this dissociation was reversed.

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ORIGINAL RESEARCH PAPER

  1. Barbera, A. J. et al. The nucleosomal surface as a docking station for Kaposi's sarcoma herpesvirus LANA. Science 311, 856–861 (2006)

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  1. Assistant Editor, Nature Reviews Neuroscience,

    Ruth Williams

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  1. Ruth Williams
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Williams, R. Hitching a lift on a histone. Nat Rev Microbiol 4, 240–241 (2006). https://doi.org/10.1038/nrmicro1407

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