Premium
The trypanosome Pumilio‐domain protein PUF7 associates with a nuclear cyclophilin and is involved in ribosomal RNA maturation
Author(s) -
Droll Dorothea,
Archer Stuart,
Fenn Katelyn,
Delhi Praveen,
Matthews Keith,
Clayton Christine
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.02.018
Subject(s) - nucleolus , ribosomal protein , biology , rna binding protein , rna , microbiology and biotechnology , ribosomal rna , cyclophilin , trypanosoma brucei , exosome complex , non coding rna , genetics , ribosome , gene , cytoplasm
Proteins with Pumilio RNA binding domains (Puf proteins) are ubiquitous in eukaryotes. Some Puf proteins bind to the 3′‐untranslated regions of mRNAs, acting to repress translation and promote degradation; others are involved in ribosomal RNA maturation. The genome of Trypanosoma brucei encodes eleven Puf proteins whose function cannot be predicted by sequence analysis. We show here that epitope‐tagged Tb PUF7 is located in the nucleolus, and associated with a nuclear cyclophilin‐like protein, Tb NCP1. RNAi targeting PUF7 reduced trypanosome growth and inhibited two steps in ribosomal RNA processing.