ArticlePloS one2011
Alanine zipper-like coiled-coil domains are necessary for homotypic dimerization of plant GAGA-factors in the nucleus and nucleolus.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 44 citations in OpenAlex.
- BASIC PENTACYSTEINE1 regulatesFrontiers in plant science · 2024Article
- Plant BBR/BPC transcription factors: unlocking multilayered regulation in development, stress and immunity.Planta · 2023Review
- Family Members Additively Repress the Ectopic Expression of BASIC PENTACYSTEINE3 to Prevent Disorders in Arabidopsis Circadian Vegetative Development.Frontiers in plant science · 2022Article
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- Fluorescent Labeling and Confocal Microcopy of Plastids and Stromules.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Knowing When to Silence: Roles of Polycomb-Group Proteins in SAM Maintenance, Root Development, and Developmental Phase Transition.International journal of molecular sciences · 2020Review
- Genome-Wide Identification and Characterization of Cucumber BPC Transcription Factors and Their Responses to Abiotic Stresses and Exogenous Phytohormones.International journal of molecular sciences · 2019Article
- Phylogenetic Analyses and GAGA-Motif Binding Studies of BBR/BPC Proteins Lend to Clues in GAGA-Motif Recognition and a Regulatory Role in Brassinosteroid Signaling.Frontiers in plant science · 2019Article
- Chromatin-Based Regulation of Plant Root Development.Frontiers in plant science · 2018Review
- How to prove the existence of metabolons?Phytochemistry reviews : proceedings of the Phytochemical Society of Europe · 2018Review
- Electromagnetic Field Seems to Not Influence Transcription via CTCT Motif in Three Plant Promoters.Frontiers in plant science · 2017Article
- Binary 2in1 Vectors Improve in Planta (Co)localization and Dynamic Protein Interaction Studies.Plant physiology · 2015Article
- The Arabidopsis GAGA-Binding Factor BASIC PENTACYSTEINE6 Recruits the POLYCOMB-REPRESSIVE COMPLEX1 Component LIKE HETEROCHROMATIN PROTEIN1 to GAGA DNA Motifs.Plant physiology · 2015Article
- Light-activated phytochrome A and B interact with members of the SPA family to promote photomorphogenesis in Arabidopsis by reorganizing the COP1/SPA complex.The Plant cell · 2015Article
- Association of polyalanine and polyglutamine coiled coils mediates expansion disease-related protein aggregation and dysfunction.Human molecular genetics · 2014Article
- Quantification of Förster resonance energy transfer by monitoring sensitized emission in living plant cells.Frontiers in plant science · 2013Review
- Unraveling the circadian clock in Arabidopsis.Plant signaling & behavior · 2013Article
- Identification of two-component system elements downstream of AHK5 in the stomatal closure response of Arabidopsis thaliana.Plant signaling & behavior · 2012Article
- Basic pentacysteine proteins mediate MADS domain complex binding to the DNA for tissue-specific expression of target genes in Arabidopsis.The Plant cell · 2012Article
- Screening for in planta protein-protein interactions combining bimolecular fluorescence complementation with flow cytometry.Plant methods · 2012Article
Corrections and comments
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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 dimers in planta. Sequence comparison uncovered that this type of domain is not restricted to BBR/BPC proteins, but is found in all kingdoms.
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