The N-terminal domain of the Drosophila retinoblastoma protein Rbf1 interacts with ORC and associates with chromatin in an E2F independent manner

Joseph Ahlander, Xiao Bo Chen, Giovanni Bosco

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

Background: The retinoblastoma (Rb) tumor suppressor protein can function as a DNA replication inhibitor as well as a transcription factor. Regulation of DNA replication may occur through interaction of Rb with the origin recognition complex (ORC). Principal Findings: We characterized the interaction of Drosophila Rb, Rbf1, with ORC. Using expression of proteins in Drosophila 52 cells, we found that an N-terminal Rbf1 fragment (amino acids 1-345) is sufficient for Rbf1 association with ORC but does not bind to dE2F1. We also found that the C-terminal half of Rbf1 (amino acids 345-845) interacts with ORC. We observed that the amino-terminal domain of Rbf1 localizes to chromatin in vivo and associates with chromosomal regions implicated in replication initiation, including colocalization with Orc2 and acetylated histone H4. Conclusions/Significance: Our results suggest that Rbf1 can associate with ORC and chromatin through domains independent of the E2F binding site. We infer that Rbf1 may play a role in regulating replication directly through its association with ORC and/or chromatin factors other than E2F. Our data suggest an important role for retinoblastoma family proteins in cell proliferation and tumor suppression through interaction with the replication initiation machinery. Copyright:

Original languageEnglish
Article numbere2831
JournalPLoS ONE
Volume3
Issue number7
DOIs
StatePublished - 30 Jul 2008
Externally publishedYes

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