alanine zipper-like coiled-coil domains are necessary for homotypic dimerization of plant gaga-factors in the nucleus and nucleolus丙氨酸zipper-like卷曲螺旋域所需的同型的二聚作用的植物gaga-factors在细胞核和核仁.pdfVIP

alanine zipper-like coiled-coil domains are necessary for homotypic dimerization of plant gaga-factors in the nucleus and nucleolus丙氨酸zipper-like卷曲螺旋域所需的同型的二聚作用的植物gaga-factors在细胞核和核仁.pdf

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alanine zipper-like coiled-coil domains are necessary for homotypic dimerization of plant gaga-factors in the nucleus and nucleolus丙氨酸zipper-like卷曲螺旋域所需的同型的二聚作用的植物gaga-factors在细胞核和核仁

Alanine Zipper-Like Coiled-Coil Domains Are Necessary for Homotypic Dimerization of Plant GAGA-Factors in the Nucleus and Nucleolus Dierk Wanke*., Mareike L. Hohenstatt.¤, Marek Dynowski., Ulrich Bloss, Andreas Hecker, Kirstin Elgass, Sabine Hummel, Achim Hahn, Katharina Caesar, Frank Schleifenbaum, Klaus Harter, Kenneth W. Berendzen ¨ ¨ Center of Plant Molecular Biology (ZMBP) Plant Physiology, University of Tubingen, Tubingen, Germany Abstract GAGA-motif binding proteins control transcriptional activation or repression of homeotic genes. Interestingly, there are no sequence similarities between animal and plant proteins. Plant BBR/BPC-proteins can be classified into two distinct groups: Previous studies have elaborated on group I members only and so little is known about group II proteins. Here, we focused on the initial characterization of AtBPC6, a group II protein from Arabidopsis thaliana. Comparison of orthologous BBR/BPC sequences disclosed two conserved signatures besides the DNA binding domain. A first peptide signature is essential and sufficient to target AtBPC6-GFP to the nucleus and nucleolus. A second domain is predicted to form a zipper-like coiled-coil structure. This novel type of domain is similar to Leucine zippers, but contains invariant alanine residues with a heptad spacing of 7 amino acids. By yeast-2-hybrid and BiFC-assays we could show that this Alanine zipper domain is essential for homotypic dimerization of group II proteins in vivo. Interhelical salt bridges and charge-stabilized hydrogen bonds between acidic and basic residues of the two monomers are predicted to form an interaction domain, which does not follow the classical knobs-into-holes zipper model. FRET-FLIM analysis of GFP/RFP-hybrid fusion proteins validates the formation of parallel d

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