Molecular Cloning and Characterization of PEBP2β, the Heterodimeric Partner of a Novel Drosophila runt-Related DNA Binding Protein PEBP2α

Transcriptional regulation of osteopontin gene in vivo by PEBP2αA/CBFA1 and ETS1 in the skeletal tissues

“…Previous reports showed no or little transactivation e ect by PEBP2b and ETS1 alone (Ogawa et al, 1993b;Thomas et al, 1997). We considered the transactivation by PEBP2b or ETS1 occurred by cooperation with endogenously expressed PEBP2aA in the recipient cells (Figure 4).…”

“…These molecules share a conserved 128-amino acid domain called the runt domain because it was initially discovered in the Drosophila pair rule gene runt . This domain mediates DNA binding as well as dimerization to PEBP2b/CBFB, which has no direct DNA binding ability, and confers enhanced DNA binding capacity to PEBP2a (Ogawa et al, 1993b;Wang et al, 1993). PEBP2a speci®cally recognizes a consensus sequence, PuACCPuCA and has been reported to control polyoma virus enhancer (Kamachi et al, 1990), murine leukemia virus enhancers , T cell-speci®c genes (Giese et al, 1995;Hallberg et al, 1992;Hsiang et al, 1993;Prosser et al, 1992;Redondo et al, 1992), enzymes (myeloperoxidase, neutrophil elastase, granzyme B serine protease) (Nuchprayoon et al, 1994;Wargnier et al, 1995) and cytokines and their receptors (GM-CSF, IL3, CSF-1) (Cameron et al, 1994;Frank et al, 1995;Zhang et al, 1994).…”

AML-1, PU.1, and Sp3 regulate expression of human bactericidal/permeability-increasing protein

“…10). Given that mutation analysis and EMSA indicated an important role of AML1, this finding was unexpected and might indicate that AML1 requires additional factors, such as CBFb [32][33][34][35] or MOZ [36], to be active. The fusion protein AML1-ETO, present in some cases of acute myeloid leukemia, functions as a strong repressor of AML1-responsive promoters in a dominant negative fashion [37][38][39][40].…”

A full-length Cbfa1 gene product perturbs T-cell development and promotes lymphomagenesis in synergy with MYC

“…The CBFA1 and CBFA2 genes are expressed in a restricted set of tissues and cell types (Ogawa et al, 1993a; while the CBFA3 gene is more widely expressed (Levanon et al, 1994). The ubiquitously expressed CBFB subunit, encoded by one gene in mammals, lacks intrinsic DNA binding activity but increases the a nity of its a-chain partner for DNA (Ogawa et al, 1993b;Wang et al, 1993).…”