High impact information on MIZF

• Using chromatin immunoprecipitation analysis and ligation-mediated PCR-assisted genomic sequencing, we show that HiNF-P interacts with conserved H4 cell cycle regulatory sequences in vivo [1].
• Here we have purified and functionally characterized the critical transcription factor HiNF-P, which is required for E2F-independent activation of the histone H4 multigene family [1].
• Antisense inhibition of HiNF-P reduces endogenous histone H4 gene expression [1].
• The biological role of HiNF-P is reflected by impeded cell cycle progression into S phase upon antisense-mediated reduction of HiNF-P levels [1].
• Decreased occupancy of site II is reflected by loss of the site II binding protein HiNF-P [2].

Biological context of MIZF

• These results suggest that MIZF, through its DNA-binding activity, acts as a sequence-specific transcriptional repressor likely involved in MBD2-mediated epigenetic gene silencing [3].
• Reporter assays demonstrated that MIZF represses transcription from the promoter including this DNA sequence [3].
• Using a cyclic amplification and selection of targets technique, the consensus sequence CGGACGTT, which contains a conserved CGGAC core, was determined as sufficient for MIZF binding [3].
• Four of seven zinc fingers present in the C-terminal region of MIZF are required for binding with MBD2 [4].
• Here, using cells synchronized in S-phase and in mitosis, as well as serum-stimulated cells, we have investigated how HiNF-P is regulated during the cell cycle and examined its stability relative to p220NPAT [5].

Anatomical context of MIZF

• The MIZF mRNA is expressed in all human tissues and cell lines examined [4].

Other interactions of MIZF

• We have recently identified a novel zinc finger protein, MIZF, as an MBD2-binding partner [3].
• The HiNF-P-dependent stabilization of p220NPAT may reinforce signaling through the cyclin E/CDK2/p220NPAT pathway and contribute to coordinate control of histone gene expression [5].

Analytical, diagnostic and therapeutic context of MIZF

• A direct interaction between MBD2 and MIZF was confirmed by in vitro binding assays and immunoprecipitation experiments [4].

References