Unique decapping complex in trypanosomes

A unique mRNA decapping complex in trypanosomes.

Kramer S, Karolak NK, Odenwald J, Gabiatti B, Castañeda Londoño PA, Zavřelová A, Freire ER, Almeida KS, Braune S, Moreira C, Eder A, Goos C, Field M, Carrington M, Holetz F, Górna MW, Zoltner M.

Nucleic Acids Research (2023) gkad497 https://doi.org/10.1093/nar/gkad497

In a joint effort together with Kramer and Zoltner labs supported by collaborators in the UK and Brasil, we described a novel mRNA decapping complex that is unique to trypanosomes. Trypanosomes are unicellular parasites causing the sleeping sickness (Human African Trypanosomiasis) and unique proteins may constitute excellent drug targets against this disease.

Natalia Karolak, a PhD candidate in our group, has purified the Trypanosoma brucei decapping enzyme ALPH1 and characterized its oligomeric state, discovering that the C-terminal domain is responsible for dimerization. Maria Górna has analyzed the predicted structure of ALPH1 and detected that the C-terminal domain comprised of α-helices resembles the GE1 domain which in other eukaryotes is responsible for interaction, oligomerization and localization to RNA granules of analogous complexes based on the usual decapping enzyme Dcp2.

News blurb in PL: CNBCh | WCh