Metabolomics,Unknown,Transcriptomics,Genomics,Proteomics

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Expression profiles and ChIP on chip genomewide experiments with deltaCR2 mutant virus

ABSTRACT: Adenovirus e1a induces quiescent human cells to divide. We found that e1a causes global relocalization of the RB-proteins (RB, p130, p107) and p300/CBP histone acetyltransferases on promoters that restricts H3K18ac to a limited set of genes to stimulate cell cycling and inhibit antiviral responses and cellular differentiation. Soon after expression, e1a binds transiently to cell cycle/growth genes, causing enrichment of p300/CBP, PCAF, H3K18ac, depletion of RB-proteins, and transcriptional activation. e1a also associates transiently with antiviral genes, causing enrichment for RB, p130, H4K16ac, increased nucleosome density, and repression. At later times, e1a and p107 bind mainly to development/differentiation genes, repressing transcription. The temporal order of e1a binding required its interactions with p300/CBP and RB-proteins. Our data uncover a defined transcriptional and epigenetic reprogramming leading to cellular transformation. Expression profiles and ChIP on chip genomewide experiments with deltaCR2 mutant virus

ORGANISM(S): Homo sapiens

SUBMITTER: Siavash Kurdistani 

PROVIDER: E-GEOD-12047 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Epigenetic reprogramming by adenovirus e1a.

Ferrari Roberto R   Pellegrini Matteo M   Horwitz Gregory A GA   Xie Wei W   Berk Arnold J AJ   Kurdistani Siavash K SK  

Science (New York, N.Y.) 20080801 5892

Adenovirus e1a induces quiescent human cells to replicate. We found that e1a causes global relocalization of the RB (retinoblastoma) proteins (RB, p130, and p107) and p300/CBP histone acetyltransferases on promoters, the effect of which is to restrict the acetylation of histone 3 lysine-18 (H3K18ac) to a limited set of genes, thereby stimulating cell cycling and inhibiting antiviral responses and cellular differentiation. Soon after expression, e1a binds transiently to promoters of cell cycle an  ...[more]

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