ArticleBMC genomics2013
Drosophila GAGA factor polyglutamine domains exhibit prion-like behavior.
Article in BMC genomics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Prion-like proteins: from computational approaches to proteome-wide analysis.FEBS open bio · 2021Review
- Generalizable Compositional Features Influencing the Proteostatic Fates of Polar Low-Complexity Domains.International journal of molecular sciences · 2021Article
- CLAMP and Zelda function together to promoteeLife · 2021Article
- Prions: Roles in Development and Adaptive Evolution.Journal of molecular evolution · 2020Review
- Natural and pathogenic protein sequence variation affecting prion-like domains within and across human proteomes.BMC genomics · 2020Article
- Differential Occupancy of Two GA-Binding Proteins Promotes Targeting of the Drosophila Dosage Compensation Complex to the Male X Chromosome.Cell reports · 2018Article
- Discovering Putative Prion-Like Proteins inFrontiers in microbiology · 2018Article
- Histone locus regulation by theGenes & development · 2017Article
- Long-term memory consolidation: The role of RNA-binding proteins with prion-like domains.RNA biology · 2017Review
- Amino acid composition predicts prion activity.PLoS computational biology · 2017Article
- The Rho Termination Factor of Clostridium botulinum Contains a Prion-Like Domain with a Highly Amyloidogenic Core.Frontiers in microbiology · 2015Article
- Spatial quality control bypasses cell-based limitations on proteostasis to promote prion curing.eLife · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe Drosophila GAGA factor (GAF) participates in nucleosome remodeling to activate genes, acts as an antirepressor and is associated with heterochromatin, contributing to gene repression. GAF functions are intimately associated to chromatin-based epigenetic control, linking basic transcriptional regulation to heritable long-term maintenance of gene expression. These diverse functions require GAF to interact with different partners in different multiprotein complexes. The two isoforms of GAF depict highly conserved glutamine-rich C-terminal domains (Q domain), which have been implicated in complex formation.
resultsHere we show that the Q domains exhibit prion-like properties. In an established yeast test system the two GAF Q domains convey prion activities comparable to well known yeast prions. The Q domains stably maintain two distinct conformational states imposing functional constraints on the fused yeast reporter protein. The prion-like phenotype can be reversibly cured in the presence of guanidine HCl or by over-expression of the Hsp104 chaperone protein. Additionally, when fused to GFP, the Q domains form aggregates in yeast cells.
conclusionWe conclude that prion-like behavior of the GAF Q domain suggests that this C-terminal structure may perform stable conformational switches. Such a self-perpetuating change in the conformation could assist GAF executing its diverse epigenetic functions of gene control in Drosophila.
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