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Trypanosomatids possess two homologues of Nopp140: a canonical Nopp140 and a Nopp140-like protein (TbNoLP) in which a GAR domain replaces the C-terminal SRP40 domain. Both are phosphorylated and coimmunoprecipitate with RNA polymerase I. Each paralogue has a distinct subnuclear localization, and depletion of TbNoLP produces an enlarged nucleolus in which TbNopp140-containing regions disperse. The restricted occurrence pattern of NoLP proteins reflects an intriguing convergence in evolution, suggestive of a function in nucleoplasmic small nucleolar ribonucleoprotein shuttling.

Original publication




Journal article


Eukaryot Cell

Publication Date





876 - 879


Amino Acid Sequence, Animals, Cell Nucleolus, Cell Nucleus, Molecular Sequence Data, Nuclear Proteins, Phosphoproteins, Phosphorylation, Protozoan Proteins, RNA Interference, RNA Polymerase I, Ribonucleoproteins, Small Nucleolar, Trypanosoma brucei brucei