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PfAlbas constitute a new eukaryotic DNA/RNA-binding protein family in malaria parasites
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 (Acet...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3326326/ https://www.ncbi.nlm.nih.gov/pubmed/22167473 http://dx.doi.org/10.1093/nar/gkr1215 |
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author | Chêne, Arnaud Vembar, Shruthi S. Rivière, Loïc Lopez-Rubio, José Juan Claes, Aurelie Siegel, T. Nicolai Sakamoto, Hiroshi Scheidig-Benatar, Christine Hernandez-Rivas, Rosaura Scherf, Artur |
author_facet | Chêne, Arnaud Vembar, Shruthi S. Rivière, Loïc Lopez-Rubio, José Juan Claes, Aurelie Siegel, T. Nicolai Sakamoto, Hiroshi Scheidig-Benatar, Christine Hernandez-Rivas, Rosaura Scherf, Artur |
author_sort | Chêne, Arnaud |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-3326326 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-33263262012-04-16 PfAlbas constitute a new eukaryotic DNA/RNA-binding protein family in malaria parasites Chêne, Arnaud Vembar, Shruthi S. Rivière, Loïc Lopez-Rubio, José Juan Claes, Aurelie Siegel, T. Nicolai Sakamoto, Hiroshi Scheidig-Benatar, Christine Hernandez-Rivas, Rosaura Scherf, Artur Nucleic Acids Res Molecular Biology 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. Oxford University Press 2012-04 2011-12-13 /pmc/articles/PMC3326326/ /pubmed/22167473 http://dx.doi.org/10.1093/nar/gkr1215 Text en © The Author(s) 2011. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Molecular Biology Chêne, Arnaud Vembar, Shruthi S. Rivière, Loïc Lopez-Rubio, José Juan Claes, Aurelie Siegel, T. Nicolai Sakamoto, Hiroshi Scheidig-Benatar, Christine Hernandez-Rivas, Rosaura Scherf, Artur PfAlbas constitute a new eukaryotic DNA/RNA-binding protein family in malaria parasites |
title | PfAlbas constitute a new eukaryotic DNA/RNA-binding protein family in malaria parasites |
title_full | PfAlbas constitute a new eukaryotic DNA/RNA-binding protein family in malaria parasites |
title_fullStr | PfAlbas constitute a new eukaryotic DNA/RNA-binding protein family in malaria parasites |
title_full_unstemmed | PfAlbas constitute a new eukaryotic DNA/RNA-binding protein family in malaria parasites |
title_short | PfAlbas constitute a new eukaryotic DNA/RNA-binding protein family in malaria parasites |
title_sort | pfalbas constitute a new eukaryotic dna/rna-binding protein family in malaria parasites |
topic | Molecular Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3326326/ https://www.ncbi.nlm.nih.gov/pubmed/22167473 http://dx.doi.org/10.1093/nar/gkr1215 |
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