Abstract
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 language | English |
|---|---|
| Pages (from-to) | 876-9 |
| Number of pages | 4 |
| Journal | Eukaryotic Cell |
| Volume | 5 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - May 2006 |
Keywords
- 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
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