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

MCM4 shares homology to a replication/DNA- binding domain in CTF and is contacted by pRb.

pRb limits the initiation of DNA replication. By immunoblotting of in vitro kinase assays we show that Cdk4,6-cyclin D contributed to pRb-phosphorylation at Ser-608, which was necessary to release pRb from chromatin in Nalm-6 cells, demonstrated by immunoprecipitations of differential cell extractions. A new binding protein of under-phosphorylated pRb, MCM4, was identified using LexA-Rb(561-660) in the two-hybrid assay. Sequence analysis revealed a novel conserved motif in MCM4's COOH-terminus with homology to the DNA-binding/viral replication activation domain of CTF/NF-I indicating their implication in the same process, and suggesting a model that CTF/NF-I stimulated binding of MCM4 to DNA, thereby to under-phosphorylated pRb. Accordingly, the pRb-MCM4-CTF/NF-I complex was immunodetected in Nalm-6 cells. Moreover, the motif was also in XPD, pointing to a collaboration of CTF/NF-I with XPD in nucleotide excision repair and in basal transcription and with MCM4 in the assembly of MCM complexes in which pRb specifically contacted MCM4.[1]

References

  1. MCM4 shares homology to a replication/DNA-binding domain in CTF and is contacted by pRb. Schmitz, N.M., Leibundgut, K., Hirt, A. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
 
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