{"database":"biostudies-other","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Prof. Artur Scherf"],"funding":["ParaFrap LabEx","FOSISS-CONACyT","Consejo Nacional de Ciencia y Tecnología (CONACYT)","European Research Council Advanced grant"],"journal":["EMBO Reports"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-SCDT-EMBOR-2018-46331-T"],"abstract":["Post-translational modifications of histone H3 N-terminal tails are key epigenetic regulators of virulence gene expression and sexual commitment in the human malaria parasite Plasmodium falciparum. Here, we identify proteolytic clipping of the N-terminal tail of nucleosome-associated histone H3 at amino acid position 21 as a new chromatin modification. A Cathepsin C-like proteolytic clipping activity is observed in nuclear parasite extracts. Notably, an ectopically expressed version of clipped histone H3, PfH3p-HA, is targeted to the nucleus and integrates into mononucleosomes. Furthermore, chromatin immunoprecipitation and next generation sequencing analysis identified PfH3p-HA as being highly enriched in the upstream region of six genes that play a key role in DNA replication and repair:"],"repository":["biostudies-other"],"funding_grant_id":["228896","272364","ANR-11-LABX0024","PlasmoSilencing 670301"],"pubmed_authors":["Dr. Beatriz Xoconostle-Cazares","Dr. Gabriela, Romero Meza","Dr. Shruthi, Shidhar Vembar","Dr. Rafael, Miyazawa Martins","Rosaura Hernandez-Rivas","Prof. Artur Scherf","Ms. Daniela Lozano-Amado","Miguel Vargas","Dr. Cameron, Ross MacPherson","Dr. Abril, Marcela Herrera-Solorio","Patty Chen"],"additional_accession":[]},"is_claimable":false,"name":"Clipped histone H3 is integrated into nucleosomes of DNA replication genes in the human malaria parasite Plasmodium falciparum","description":"Post-translational modifications of histone H3 N-terminal tails are key epigenetic regulators of virulence gene expression and sexual commitment in the human malaria parasite Plasmodium falciparum. Here, we identify proteolytic clipping of the N-terminal tail of nucleosome-associated histone H3 at amino acid position 21 as a new chromatin modification. A Cathepsin C-like proteolytic clipping activity is observed in nuclear parasite extracts. Notably, an ectopically expressed version of clipped histone H3, PfH3p-HA, is targeted to the nucleus and integrates into mononucleosomes. Furthermore, chromatin immunoprecipitation and next generation sequencing analysis identified PfH3p-HA as being highly enriched in the upstream region of six genes that play a key role in DNA replication and repair:","dates":{"release":"2020-01-16T21:00:10Z","modification":"2020-01-16T21:00:10Z","creation":"2020-01-16T21:00:10Z"},"accession":"S-SCDT-EMBOR-2018-46331-T","cross_references":{"doi":["10.15252/embr.201846331"]}}