High impact information on Ebf1

• The Olf-1 protein, expressed exclusively in the olfactory receptor neurons and their precursors, contains a new helix-loop-helix motif and functions as an apparent homodimer [1].
• An additional role for the Roaz/Olf-1/EBF heterodimeric protein is suggested by its ability to regulate gene activation at a distinct promoter lacking Olf-1/EBF-binding sites [2].
• Analysis of the structural requirement for protein dimerization and DNA binding by Roaz reveals the role of specific zinc finger motifs in the Roaz protein for homodimerization and heterodimerization with the Olf-1/EBF transcription factor [2].
• The Olf-1 binding sites described define the consensus sequence YTCCCYRGGGAR [3].
• These experiments support a model in which expression of Olf-1 in the sensory neurons coordinately activates a set of olfactory neuron-specific genes [3].

Anatomical context of Ebf1

• The transcription factor Olf-1 was found to be highly expressed in the olfactory epithelium and was detected at a similar level in the vomeronasal epithelium [4].

Associations of Ebf1 with chemical compounds

• A highly ordered, electrostatic network containing 7 hydrogen (H)-bonds links the OE1 and OE2 atoms of myristate's carboxylate group, the indole nitrogen of Trp82, NH1, and NH2 of Arg106, NE2, and OE1 of Gln115, and 2 interior ordered waters [5].

Analytical, diagnostic and therapeutic context of Ebf1

• Molecular cloning of the olfactory neuronal transcription factor Olf-1 by genetic selection in yeast [1].

References