Publications by authors named "Paula Andrea Castaneda Londono"
Article Synopsis
- The removal of the mRNA 5' cap is key for gene expression regulation and leads to transcript degradation in eukaryotes.
- Unlike other eukaryotes, Kinetoplastida, such as T. brucei, use the ALPH1 enzyme for decapping instead of the typical Dcp2 enzyme, and ALPH1 forms complexes with several unique Kinetoplastida proteins.
- The structure and localization of ALPH1, particularly its C- and N-terminal regions, are crucial for its interaction with other proteins and RNA granules, indicating distinct regulatory mechanisms compared to other organisms.
Background: ApaH like phosphatases (ALPHs) originate from the bacterial ApaH protein and have been identified in all eukaryotic super-groups. Only two of these proteins have been functionally characterised. We have shown that the ApaH like phosphatase ALPH1 from the Kinetoplastid Trypanosoma brucei is the mRNA decapping enzyme of the parasite.
View Article and Find Full Text PDFWe analysed a widely used barcode, the V9 region of the 18S rRNA gene, to study the effect of environmental conditions on the distribution of two related heterotrophic protistan lineages in marine plankton, kinetoplastids and diplonemids. We relied on a major published dataset (Tara Oceans) where samples from the mesopelagic zone were available from just 32 of 123 locations, and both groups are most abundant in this zone. To close sampling gaps and obtain more information from the deeper ocean, we collected 57 new samples targeting especially the mesopelagic zone.
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