ArticleNucleic acids research2012
PfAlbas constitute a new eukaryotic DNA/RNA-binding protein family in malaria parasites.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- GID/CTLH E3 ligase complex control cell fate programs for sexual development of Plasmodium falciparum.Nature communications · 2026Article
- Ectopic overexpression ofMicrobiology spectrum · 2025Article
- Genome-wide identification and characterization of the ALBA gene family in rapeseed (Frontiers in plant science · 2025Article
- Evolution of sequence, structural and functional diversity of the ubiquitous DNA/RNA-binding Alba domain.Scientific reports · 2024Article
- The DEAD-box RNA helicase PfDOZI imposes opposing actions on RNA metabolism in Plasmodium falciparum.Nature communications · 2024Article
- Article
- Immunoprecipitation of RNA-DNA hybrid interacting proteins in Trypanosoma brucei reveals conserved and novel activities, including in the control of surface antigen expression needed for immune evasion by antigenic variation.Nucleic acids research · 2023Article
- Discovery of RUF6 ncRNA-interacting proteins involved inLife science alliance · 2023Article
- ALBA proteins confer thermotolerance through stabilizing HSF messenger RNAs in cytoplasmic granules.Nature plants · 2022Article
- The Putative Bromodomain Protein PfBDP7 of the Human Malaria ParasiteFrontiers in cell and developmental biology · 2022Article
- Malaria Parasite Stress Tolerance Is Regulated by DNMT2-Mediated tRNA Cytosine Methylation.mBio · 2021Article
- Pb103 Regulates Zygote/Ookinete Development inPathogens (Basel, Switzerland) · 2021Article
- Phage Display Screening for Alba Superfamily Proteins from the Human Malaria Parasite, Plasmodium falciparum Reveals a High Level of Association with Protein Modification Pathways and Hints at New Drug Targets.Acta parasitologica · 2021Article
- An Alba-domain protein required for proteome remodelling during trypanosome differentiation and host transition.PLoS pathogens · 2021Article
- Core spliceosomal Sm proteins as constituents of cytoplasmic mRNPs in plants.The Plant journal : for cell and molecular biology · 2020Article
- Exploring the virulence gene interactome with CRISPR/dCas9 in the human malaria parasite.Molecular systems biology · 2020Article
- Discovery of a new predominant cytosine DNA modification that is linked to gene expression in malaria parasites.Nucleic acids research · 2020Article
- Unraveling the 3D genome of human malaria parasites.Seminars in cell & developmental biology · 2019Review
- Genome-wide real-time in vivo transcriptional dynamics during Plasmodium falciparum blood-stage development.Nature communications · 2018Article
- Article
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10 authors.
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Abstract
In Plasmodium falciparum, perinuclear subtelomeric chromatin conveys monoallelic expression of virulence genes. However, proteins that directly bind to chromosome ends are poorly described. Here we identify a novel DNA/RNA-binding protein family that bears homology to the archaeal protein Alba (Acetylation lowers binding affinity). We isolated three of the four PfAlba paralogs as part of a molecular complex that is associated with the P. falciparum-specific TARE6 (Telomere-Associated Repetitive Elements 6) subtelomeric region and showed in electromobility shift assays (EMSAs) that the PfAlbas bind to TARE6 repeats. In early blood stages, the PfAlba proteins were enriched at the nuclear periphery and partially co-localized with PfSir2, a TARE6-associated histone deacetylase linked to the process of antigenic variation. The nuclear location changed at the onset of parasite proliferation (trophozoite-schizont), where the PfAlba proteins were also detectable in the cytoplasm in a punctate pattern. Using single-stranded RNA (ssRNA) probes in EMSAs, we found that PfAlbas bind to ssRNA, albeit with different binding preferences. We demonstrate for the first time in eukaryotes that Alba-like proteins bind to both DNA and RNA and that their intracellular location is developmentally regulated. Discovery of the PfAlbas may provide a link between the previously described subtelomeric non-coding RNA and the regulation of antigenic variation.
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