Two distinct classes of CCAAT box elements that bind nuclear factor-Y/alpha-actinin-4: potential role in human CYP1A1 regulation
Abstract
A negative regulatory element (NRE1; position -794 to -774) was previously identified that mediates the downregulation of CYP1A1, including partial suppression of Ah receptor-dependent induction. The CCAAT-box binding protein, nuclear factor-Y (NF-Y), is a component of one of two protein complexes that specifically and competitively bind the CYP1A1 NRE1 in vitro with nearly equal affinity. The second complex involves an unidentified protein(s) called the negative regulatory factor (NRF). Competitive electrophoretic mobility shift assays (EMSA) revealed two distinct classes of NF-Y-binding CCAAT-box elements distinguished by their ability or inability to also bind NRF. To further explore the identity of NRE1-binding proteins, a purification scheme was developed culminating in NRE1-dependent DNA affinity chromatography and sequence analysis. An approximate 106-kDa protein was purified and shown to be alpha-actinin-4 (ACTN4), one of two ubiquitously expressed non-muscle actinins. Electrophoretic mobility shift assays combined with Western blot analysis and co-immunoprecipitation experiments suggested that ACTN4 is associated with the NF-Y complex, but not NRF. Attempts to demonstrate a role for NF-Y/ACTN4 in regulating CYP1A1 expr...Continue Reading
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Identification of two domains of the p70 Ku protein mediating dimerization with p80 and DNA binding.
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