EBF contains a novel zinc coordination motif and multiple dimerization and transcriptional activation domains.

摘要: Abstract Early B cell factor (EBF) was identified and cloned as a transcription expressed specifically in lymphocytes adipocytes. This protein also olfactory 1 (Olf-1) neurons. In this study, we analyzed the structural requirements for DNA binding, homodimerization transcriptional activation by EBF. A carboxyl-terminal region, containing repeat of alpha-helices related to helix-loop-helix motif, is important dimerization EBF solution can confer upon heterologous binding protein. The amino-terminal domain itself monomeric, but mediate assembly dimers on optimized correctly spaced half-sites. Mutational analysis indicated that novel zinc coordination motif consisting H-X3-C-X2-C-X5-C recognition. Deletion transfer regions onto serine/threonine-rich domain. Moreover, from sites. Thus, contains both complex allows activation, additional domains.