The N-terminal domain of the Drosophila retinoblastoma protein Rbf1 interacts with ORC and associates with chromatin in an E2F independent manner.
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...
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2008-07-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC2475671?pdf=render |
| _version_ | 1811330695861108736 |
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| author | Joseph Ahlander Xiao-Bo Chen Giovanni Bosco |
| author_facet | Joseph Ahlander Xiao-Bo Chen Giovanni Bosco |
| author_sort | Joseph Ahlander |
| collection | DOAJ |
| description | 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 S2 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. |
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| format | Article |
| id | doaj.art-2282d706584c4c3d82e8e11293984eea |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-04-13T16:06:27Z |
| publishDate | 2008-07-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-2282d706584c4c3d82e8e11293984eea2022-12-22T02:40:22ZengPublic Library of Science (PLoS)PLoS ONE1932-62032008-07-0137e283110.1371/journal.pone.0002831The N-terminal domain of the Drosophila retinoblastoma protein Rbf1 interacts with ORC and associates with chromatin in an E2F independent manner.Joseph AhlanderXiao-Bo ChenGiovanni BoscoBACKGROUND: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 S2 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.http://europepmc.org/articles/PMC2475671?pdf=render |
| spellingShingle | Joseph Ahlander Xiao-Bo Chen Giovanni Bosco The N-terminal domain of the Drosophila retinoblastoma protein Rbf1 interacts with ORC and associates with chromatin in an E2F independent manner. PLoS ONE |
| title | The N-terminal domain of the Drosophila retinoblastoma protein Rbf1 interacts with ORC and associates with chromatin in an E2F independent manner. |
| title_full | The N-terminal domain of the Drosophila retinoblastoma protein Rbf1 interacts with ORC and associates with chromatin in an E2F independent manner. |
| title_fullStr | The N-terminal domain of the Drosophila retinoblastoma protein Rbf1 interacts with ORC and associates with chromatin in an E2F independent manner. |
| title_full_unstemmed | The N-terminal domain of the Drosophila retinoblastoma protein Rbf1 interacts with ORC and associates with chromatin in an E2F independent manner. |
| title_short | The N-terminal domain of the Drosophila retinoblastoma protein Rbf1 interacts with ORC and associates with chromatin in an E2F independent manner. |
| title_sort | n terminal domain of the drosophila retinoblastoma protein rbf1 interacts with orc and associates with chromatin in an e2f independent manner |
| url | http://europepmc.org/articles/PMC2475671?pdf=render |
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