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 Citations (Scopus)

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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Origin Recognition Complex
Drosophila Proteins
Retinoblastoma Protein
Chromatin
chromatin
Drosophila
DNA replication
amino acids
family relations
proteins
Retinoblastoma
DNA Replication
histones
binding sites
cell proliferation
transcription factors
protein synthesis
Tumor Suppressor Proteins
Amino Acids
neoplasms

Cite this

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title = "The N-terminal domain of the Drosophila retinoblastoma protein Rbf1 interacts with ORC and associates with chromatin in an E2F independent manner",
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:",
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The N-terminal domain of the Drosophila retinoblastoma protein Rbf1 interacts with ORC and associates with chromatin in an E2F independent manner. / Ahlander, Joseph; Chen, Xiao Bo; Bosco, Giovanni.

In: PLoS ONE, Vol. 3, No. 7, e2831, 30.07.2008.

Research output: Contribution to journalArticle

TY - JOUR

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AB - 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:

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