| Title | Subnuclear distribution of the largest subunit of the human origin recognition complex during the cell cycle |
|---|---|
| Publication Type | Articolo su Rivista peer-reviewed |
| Year of Publication | 2004 |
| Authors | Lidonnici, M.R., Rossi R., Paixão S., Mendoza-Maldonado R., Paolinelli R., Arcangeli Caterina, Giacca M., Biamonti G., and Montecucco A. |
| Journal | Journal of Cell Science |
| Volume | 117 |
| Pagination | 5221-5231 |
| ISSN | 00219533 |
| Keywords | Adenosine Triphosphate, amino terminal sequence, animal cell, Animalia, Animals, article, binding site, Binding Sites, Biological, Blotting, Cell cycle, cell cycle G1 phase, cell cycle S phase, Cell Line, Cell Nucleus, cellular distribution, chromatin, controlled study, COS Cells, DNA Replication, DNA-Binding Proteins, Eukaryota, fluorescence, fluorescence resonance energy transfer, gene overexpression, Glutathione Transferase, Green Fluorescent Proteins, Hela Cells, heterochromatin, heterochromatin protein 1, human, human cell, Humans, Immunoprecipitation, in vitro study, in vivo study, Mice, Microscopy, Models, mutation, NIH 3T3 Cells, nonhuman, nuclear protein, Origin Recognition Complex, Pancreatic, Plasmids, Polymerase Chain Reaction, priority journal, protein binding, protein degradation, protein domain, protein localization, protein orc1, protein protein interaction, Protein Structure, protein subunit, protein synthesis, Ribonuclease, S Phase, Tertiary, Time Factors, Transfection, unclassified drug, Western |
| Abstract | In eukaryotes, initiation of DNA replication requires the activity of the origin recognition complex (ORC). The largest subunit of this complex, Orc1p, has a critical role in this activity. Here we have studied the subnuclear distribution of the overexpressed human Orc1p during the cell cycle. Orc1p is progressively degraded during S-phase according to a spatio-temporal program and it never colocalizes with replication factories. Orc1p is resynthesized in G1. In early G1, the protein is distributed throughout the cell nucleus, but successively it preferentially associates with heterochromatin. This association requires a functional ATP binding site and a protein region partially overlapping the bromo-adjacent homology domain at the N-terminus of Orc1p. The same N-terminal region mediates the in vitro interaction with heterochromatin protein 1 (HP1). Fluorescence resonance energy transfer (FRET) experiments demonstrate the interaction of human Orc1p and HP1 in vivo. Our data suggest a role of HP1 in the recruitment but not in the stable association of Orc1p with heterochromatin. Indeed, the subnuclear distribution of Orc1p is not affected by treatment that trigger the dispersal of HP1. |
| Notes | cited By 35 |
| URL | https://www.scopus.com/inward/record.uri?eid=2-s2.0-9444263732&doi=10.1242%2fjcs.01405&partnerID=40&md5=0937f1cceceab414e202ba9bdee7fd84 |
| DOI | 10.1242/jcs.01405 |
| Citation Key | Lidonnici20045221 |
