RNase III Domain of KREPB9 and KREPB10 Association with Editosomes in Trypanosoma brucei.

ABSTRACT: Editosomes are the multiprotein complexes that catalyze the insertion and deletion of uridines to create translatable mRNAs in the mitochondria of kinetoplastids. Recognition and cleavage of a broad diversity of RNA substrates in vivo require three functionally distinct RNase III-type endonucleases, as well as five additional editosome proteins that contain noncatalytic RNase III domains. RNase III domains have recently been identified in the editosome accessory proteins KREPB9 and KREPB10, suggesting a role related to editing endonuclease function. In this report, we definitively show that KREPB9 and KREPB10 are not essential in either bloodstream-form parasites (BF) or procyclic-form parasites (PF) by creating null or conditional null cell lines. While preedited and edited transcr

SUBMITTER: Carnes J 

PROVIDER: S-EPMC5770545 | biostudies-literature | 2018 Jan-Feb

REPOSITORIES: biostudies-literature