Abstract
| Original language | English |
|---|---|
| Article number | e16070 |
| Number of pages | 15 |
| Journal | PLoS ONE |
| Volume | 6 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2011 |
| Externally published | Yes |
Cite this
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Alanine zipper-like coiled-coil domains are necessary for homotypic dimerization of plant GAGA-factors in the nucleus and nucleolus. / Wanke, Dierk; Hohenstatt, Mareike L; Dynowski, Marek; Bloss, Ulrich; Hecker, Andreas; Elgass, Kirstin; Hummel, Sabine; Hahn, Achim; Caesar, Katharina; Schleifenbaum, Frank E; Harter, Klaus; Berendzen, Kenneth Wayne.
In: PLoS ONE, Vol. 6, No. 2, e16070, 2011.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - Alanine zipper-like coiled-coil domains are necessary for homotypic dimerization of plant GAGA-factors in the nucleus and nucleolus
AU - Wanke, Dierk
AU - Hohenstatt, Mareike L
AU - Dynowski, Marek
AU - Bloss, Ulrich
AU - Hecker, Andreas
AU - Elgass, Kirstin
AU - Hummel, Sabine
AU - Hahn, Achim
AU - Caesar, Katharina
AU - Schleifenbaum, Frank E
AU - Harter, Klaus
AU - Berendzen, Kenneth Wayne
PY - 2011
Y1 - 2011
N2 - 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 dimers in planta. Sequence comparison uncovered that this type of domain is not restricted to BBR/BPC proteins, but is found in all kingdoms.
AB - 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 dimers in planta. Sequence comparison uncovered that this type of domain is not restricted to BBR/BPC proteins, but is found in all kingdoms.
UR - http://www.ncbi.nlm.nih.gov/pubmed/21347358
U2 - 10.1371/journal.pone.0016070
DO - 10.1371/journal.pone.0016070
M3 - Article
VL - 6
JO - PLoS ONE
JF - PLoS ONE
SN - 1932-6203
IS - 2
M1 - e16070
ER -