Characterization and functional analysis of CReMM, a novel chromodomain helicase DNA-binding protein

I. Shur, D. Benayahu

Research output: Contribution to journalArticlepeer-review


The present study describes a newly identified protein named CReMM (chromatin-related mesenchymal modulator). The protein was studied by bioinformatic means and classified as a member of the third subfamily of chromodomain helicase DNA-binding proteins (CHD). In silico translation defined CReMM as a multiple domains protein including two chromodomains, SNF2/ATPase, helicase C domain and an A/T-DNA-binding domain (DBD). Predicted extensive post-translation phosphorylation on serine and tyrosine residues was demonstrated by Western blot in the presence and in the absence of phosphatase inhibitors using specific antibodies. Immunoprecipitated CReMM disclosed a DNA-dependent ATPase activity quantified by colorimetric assay. Electrophoresis mobility-shift assay (EMSA) validated that CReMM binds to A/T-rich DNA. CReMM is expressed in mesenchymal progenitors, as shown in vitro and in vivo. CReMM protein structural motifs and proven biochemical activities highlight its role in chromatin remodeling. Further delineation of the function of this protein will provide information about its dynamics in transcriptional regulation of mesenchymal cells.

Original languageEnglish
Pages (from-to)646-655
Number of pages10
JournalJournal of Molecular Biology
Issue number3
StatePublished - 23 Sep 2005


  • ATPase
  • Chromodomain
  • DNA binding
  • Mesenchymal progenitors
  • Novel gene


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