Functional characterization of the trypanosome translational repressor SCD6

Cristodero, Marina; Schimanski, Bernd; Heller, Manfred; Roditi, Isabel (2014). Functional characterization of the trypanosome translational repressor SCD6. Biochemical journal, 457(1), pp. 57-67. Portland Press 10.1042/BJ20130747

[img] Text
Christodero.pdf - Published Version
Restricted to registered users only
Available under License Publisher holds Copyright.

Download (1MB) | Request a copy

The storage of translationally inactive mRNAs in cytosolic granules enables cells to react flexibly to environmental changes. In eukaryotes, Scd6 (suppressor of clathrin deficiency 6)/Rap55 (RNA-associated protein 55), a member of the LSm14 (like-Sm14) family, is an important factor in the formation and activity of P-bodies, where mRNA decay factors accumulate, in stress granules that store mRNAs under adverse conditions and in granules that store developmentally regulated mRNAs. SCD6 from Trypanosoma brucei (TbSCD6) shares the same domain architecture as orthologous proteins in other organisms and is also present in cytosolic granules (equivalent to P-bodies). We show that TbSCD6 is a general repressor of translation and that its depletion by RNAi results in a global increase in protein synthesis. With few exceptions, the steady-state levels of proteins are unchanged. TbSCD6 is not required for the formation of starvation-induced granules in trypanosomes, and unlike Scd6 from yeast, Plasmodium and all multicellular organisms analysed to date, it does not form a complex with the helicase Dhh1 (DExD/H-box helicase 1). In common with Xenopus laevis RAP55, TbSCD6 co-purifies with two arginine methyltransferases; moreover, TbSCD6 itself is methylated on three arginine residues. Finally, a detailed analysis identified roles for the Lsm and N-rich domains in both protein localization and tr

Item Type:

Journal Article (Original Article)


08 Faculty of Science > Department of Biology > Institute of Cell Biology
04 Faculty of Medicine > Pre-clinic Human Medicine > BioMedical Research (DBMR)

UniBE Contributor:

Cristodero, Marina, Schimanski, Bernd, Heller, Manfred, Roditi, Isabel


500 Science > 570 Life sciences; biology
600 Technology > 610 Medicine & health




Portland Press


[4] Swiss National Science Foundation ; [UNSPECIFIED] Howard Hughes Medical Institute ; [UNSPECIFIED] Canton of Bern




Isabel Roditi

Date Deposited:

08 May 2015 11:07

Last Modified:

05 Dec 2022 14:47

Publisher DOI:


PubMed ID:





Actions (login required)

Edit item Edit item
Provide Feedback