PubMed Journals: J Mol Biol

  Source:		PMID: 12787665

    		J Mol Biol. 2003 Jun 13;329(4):631-44.
			Functional domains of FOXJ2.

			Gómez-Ferrería MA(1), Rey-Campos J.

			Author Information
			(1) Departamento de Biología Celular y Desarrollo,
			Centro de Investigaciones Biológicas, Consejo
			Superior de Investigaciones Científicas
			(CSIC), Velázquez 144, 28006, Madrid, Spain.

			FOXJ2 is a fork head transcriptional activator,
			the expression of which starts very early
			in embryonic development and it is distributed
			widely in the adult. Here, we describe the
			characterization of domains that are important
			for its function. FOXJ2 is localized constitutively
			at the nucleus of the cell. Two tyrosine
			residues and a stretch of basic amino acid
			residues at the N and C-terminal ends of the
			fork head domain, respectively, are important
			for its nuclear targeting. These residues
			are conserved strongly among all members
			of the fork head family, suggesting that
			they could be involved in the nuclear translocation
			mechanism of all fork head factors. In addition
			to the AB domain, we have found, at least,
			two other transactivation domains: Domain
			I, at the N terminus, and the H/P domain,
			rich in histidine and proline residues.
			Although the AB domain shows the strongest
			transactivation capacity, all three domains
			are required for full FOXJ2 transcriptional
			activity. Furthermore, a fourth region rich
			in proline and glutamine residues and with
			no intrinsic transactivation function, the
			P/Q domain, appears to play an important
			role in the FOXJ2-mediated transactivation
			mechanism. Although FOXJ2 can be phosphorylated
			in two serine residues, this post-translational
			modification did not appear to be essential
			for transactivation. Finally, we have found
			that the W2 wing of the fork head domain
			of FOXJ2 is dispensable for specific DNA
			binding, although it could have a weak stabilizing
			role for the DNA-FOXJ2 complex.

			PMID: 12787665 [Indexed for MEDLINE]

     			                         Tweet       Print