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- 저자 : Ficner, Ralf (검색결과 1 건)
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The Velvet Family of Fungal Regulators Contains a DNA-Binding Domain Structurally Similar to NF-κB
Ahmed, Yasar Luqman,Gerke, Jennifer,Park, Hee-Soo,Bayram, Ö,zgü,r,Neumann, Piotr,Ni, Min,Dickmanns, Achim,Kim, Sun Chang,Yu, Jae-Hyuk,Braus, Gerhard H.,Ficner, Ralf Public Library of Science 2013 PLoS biology Vol.11 No.12
<P>Morphological development of fungi and their combined production of secondary metabolites are both acting in defence and protection. These processes are mainly coordinated by <I>velvet</I> regulators, which contain a yet functionally and structurally uncharacterized <I>velvet</I> domain. Here we demonstrate that the <I>velvet</I> domain of VosA is a novel DNA-binding motif that specifically recognizes an 11-nucleotide consensus sequence consisting of two motifs in the promoters of key developmental regulatory genes. The crystal structure analysis of the VosA <I>velvet</I> domain revealed an unforeseen structural similarity with the Rel homology domain (RHD) of the mammalian transcription factor NF-κB. Based on this structural similarity several conserved amino acid residues present in all <I>velvet</I> domains have been identified and shown to be essential for the DNA binding ability of VosA. The <I>velvet</I> domain is also involved in dimer formation as seen in the solved crystal structures of the VosA homodimer and the VosA-VelB heterodimer. These findings suggest that defence mechanisms of both fungi and animals might be governed by structurally related DNA-binding transcription factors.</P><P><B>Author Summary</B></P><P>In many fungi, developmental processes and the synthesis of nonessential chemicals (secondary metabolites) are regulated by various external stimuli, such as light. Although fungi employ them for defensive purposes, secondary metabolites range from useful antibiotics to powerful toxins, so understanding the molecular processes that regulate their synthesis is of particular interest to us. In the mold <I>Aspergillus nidulans</I> the main regulators of these processes are the so-called “<I>velvet</I>” proteins VeA, VelB, and VosA, which share a 150-amino acid region known as the <I>velvet</I> domain. <I>Velvet</I> proteins interact with each other, alone (“homodimers”), in various combinations (“heterodimers”), and also with other proteins, but the molecular mechanism by which these proteins exert their regulatory function has been unclear. In this work we show that <I>velvet</I> proteins form a family of fungus-specific transcription factors that directly bind to target DNA, even though analysis of their amino acid sequence does not reveal any known DNA-binding domains or motifs. We determined the three-dimensional structure of the VosA-VosA homodimer and the VosA-VelB heterodimer and found that the structure of the <I>velvet</I> domain is strongly reminiscent of the N-terminal immunoglobulin-like domain found in the mammalian transcription factor NFκB-p50, despite the very low sequence similarity. We propose that, like NFκB, various homo- or heterodimers of <I>velvet</I> proteins modulate gene expression to drive development and defensive pathways in fungi.</P>
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