Identification of a Novel 81-kDa Component of the Xenopus Origin Recognition Complex
The Xenopus origin recognition complex is essential for chromosomal DNA replication in cell-free extracts. We have immunopurified the Xenopus origin recognition complex with anti-Xorc2 antibodies and analyzed its composition and properties. Xorc2 (p63) is specifically associated with Xorc1 (p115) an...
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| Veröffentlicht in: | The Journal of biological chemistry 1998-09, Vol.273 (38), p.24891-24897 |
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| container_issue | 38 |
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| container_title | The Journal of biological chemistry |
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| creator | Carpenter, Phillip B. Dunphy, William G. |
| description | The Xenopus origin recognition complex is essential for chromosomal DNA replication in cell-free extracts. We have immunopurified the Xenopus origin recognition complex with anti-Xorc2 antibodies and analyzed its composition and properties. Xorc2 (p63) is specifically associated with Xorc1 (p115) and up to four additional polypeptides (p81, p78, p45, and p40). The cDNA encoding p81 is highly homologous to various expressed sequence tags from humans and mice encoding a protein of previously unknown function. Immunodepletion of p81 fromXenopus egg extracts, which also results in the removal of Xorc2, completely abolishes chromosomal DNA replication. Thus, p81 appears to play a crucial role at S phase in higher eukaryotes. |
| doi_str_mv | 10.1074/jbc.273.38.24891 |
| format | Article |
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We have immunopurified the Xenopus origin recognition complex with anti-Xorc2 antibodies and analyzed its composition and properties. Xorc2 (p63) is specifically associated with Xorc1 (p115) and up to four additional polypeptides (p81, p78, p45, and p40). The cDNA encoding p81 is highly homologous to various expressed sequence tags from humans and mice encoding a protein of previously unknown function. Immunodepletion of p81 fromXenopus egg extracts, which also results in the removal of Xorc2, completely abolishes chromosomal DNA replication. 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We have immunopurified the Xenopus origin recognition complex with anti-Xorc2 antibodies and analyzed its composition and properties. Xorc2 (p63) is specifically associated with Xorc1 (p115) and up to four additional polypeptides (p81, p78, p45, and p40). The cDNA encoding p81 is highly homologous to various expressed sequence tags from humans and mice encoding a protein of previously unknown function. Immunodepletion of p81 fromXenopus egg extracts, which also results in the removal of Xorc2, completely abolishes chromosomal DNA replication. 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| ispartof | The Journal of biological chemistry, 1998-09, Vol.273 (38), p.24891-24897 |
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| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Base Sequence Chromosomes - genetics Cloning, Molecular DNA Replication DNA, Complementary DNA-Binding Proteins - biosynthesis DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics Female Humans Mice Molecular Sequence Data Molecular Weight Oocytes - physiology Oocytes - ultrastructure Origin Recognition Complex Peptide Fragments - chemistry Phosphates - metabolism Polymerase Chain Reaction Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Sequence Tagged Sites Xenopus |
| title | Identification of a Novel 81-kDa Component of the Xenopus Origin Recognition Complex |
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