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Eukaryotic Cell, May 2006, p. 876-879, Vol. 5, No. 5
1535-9778/06/$08.00+0 doi:10.1128/EC.5.5.876-879.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, United Kingdom,1 Department of Biological Sciences, University of Hull, Cottingham Road, Hull HU6 7RX, United Kingdom2
Received 20 December 2005/ Accepted 8 March 2006
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.
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