Two novel proteins that bind specifically to the human transferrin receptor (TR promoter, have been isolated previously from HeLa cell nuclear. TREF1 and TREF2, which have apparent molecular weights of 82Kd and 62Kd respectively, appears to be associa...
Two novel proteins that bind specifically to the human transferrin receptor (TR promoter, have been isolated previously from HeLa cell nuclear. TREF1 and TREF2, which have apparent molecular weights of 82Kd and 62Kd respectively, appears to be associated as a heterocomplex and interacts specifically with a region of the TR promoter which contains the key regulatory element for the expression of TR in response to a mitogenic stimulus. The element is similar in sequence to the cAMP-responsive and phobol ester-responsive elements found in several viral and cellular genes.
In the work described in this paper, cDNA encoding the TREF2 has been isolated by screening a human cDNA library with degenerate sets of oligonucleotide derived from the amino acid sequence of tryptic peptide of TREF2.