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Ciz1, a p21 Cip1/Waf1 ‐interacting zinc finger protein and DNA replication factor, is a novel molecular partner for human enhancer of rudimentary homolog
Author(s) -
Łukasik Anna,
Uniewicz Katarzyna A.,
Kulis Marta,
Kozlowski Piotr
Publication year - 2008
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2007.06203.x
Subject(s) - zinc finger , enhancer , biology , transcription factor , origin recognition complex , dna replication , replication factor c , nuclear protein , eukaryotic dna replication , gene , microbiology and biotechnology , genetics
Enhancer of rudimentary homolog ( Drosophila ) (ERH) is a small, highly conserved, nuclear protein with a unique three‐dimensional structure, whose gene has been identified in animals, plants and protists, but not in fungi. Involvement of ERH in fundamental processes such as regulation of pyrimidine metabolism, cell cycle progression, transcription and cell growth control has been suggested. Here, employing a yeast two‐hybrid system, a glutathione S ‐transferase pull‐down assay and tandem MS, we demonstrate that Ciz1 is a bona fide interactor of human ERH. Ciz1 is a nuclear zinc finger protein interacting with p21 Cip1/Waf1 , a universal inhibitor of cyclin‐dependent kinases, and is a DNA replication factor. The region of Ciz1 necessary for the interaction with ERH spans residues 531–644, encompassing its first zinc finger motif. This region overlaps the p21 Cip1/Waf1 ‐binding site, suggesting that the interaction with ERH could block the binding of p21 Cip1/Waf1 by Ciz1 in the cell. When ERH and Ciz1 are coexpressed in HeLa cells, Ciz1 recruits ERH to DNA replication foci.