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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

Orc1  -  origin recognition complex, subunit 1

Mus musculus

Synonyms: AA545195, MmORC1, Orc1l, Origin recognition complex subunit 1
 
 
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High impact information on Orc1l

  • Immunoblotting analysis revealed that hamster Orc1 and Orc2 proteins were present in nuclei at equivalent concentrations throughout the cell cycle, but only Orc2 was stably bound to chromatin [1].
  • Since hamster Orc proteins are closely related to their human and mouse homologs, the unexpected behavior of hamster Orc1 provides a novel mechanism in mammals for delaying assembly of pre-replication complexes until mitosis is complete and a nuclear structure has formed [1].
  • ChIP assays revealed that both replication origins bind AlF-C and Orc1 [2].
  • The variant form of Orc1, Orc1B, lacks 35 amino acid residues in exon 5; the variant of Orc2, Orc2B, lacks 48 amino acid residues in exon 2 [3].
 

Analytical, diagnostic and therapeutic context of Orc1l

  • Chromatin immunoprecipitation (ChIP) assays indicated that the reduction of replicator activity was paralleled with the reduced binding of AlF-C and Orc1, suggesting that sequence-specific binding of AlF-C to the ectopic rat origin leads to enhanced replicator activity in cooperation with Orc1 [2].

References

  1. Selective instability of Orc1 protein accounts for the absence of functional origin recognition complexes during the M-G(1) transition in mammals. Natale, D.A., Li, C.J., Sun, W.H., DePamphilis, M.L. EMBO J. (2000) [Pubmed]
  2. Binding of AlF-C, an Orc1-Binding Transcriptional Regulator, Enhances Replicator Activity of the Rat Aldolase B Origin. Minami, H., Takahashi, J., Suto, A., Saitoh, Y., Tsutsumi, K. Mol. Cell. Biol. (2006) [Pubmed]
  3. Novel splicing variant of mouse Orc1 is deficient in nuclear translocation and resistant for proteasome-mediated degradation. Miyake, Y., Mizuno, T., Yanagi, K., Hanaoka, F. J. Biol. Chem. (2005) [Pubmed]
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