Functional characterization of C. elegans Y-box-binding proteins reveals tissue-specific functions and a critical role in the formation of polysomes.
The cold shock domain is one of the most highly conserved motifs between bacteria and higher eukaryotes. Y-box-binding proteins represent a subfamily of cold shock domain proteins with pleiotropic functions, ranging from transcription in the nucleus to translation in the cytoplasm. These proteins have been investigated in all major model organisms except Caenorhabditis elegans. In this study, we set out to fill this gap and present a functional characterization of CEYs, the C. elegans Y-box-binding proteins. We find that, similar to other organisms, CEYs are essential for proper gametogenesis. However, we also report a novel function of these proteins in the formation of large polysomes in the soma. In the absence of the somatic CEYs, polysomes are dramatically reduced with a simultaneous increase in monosomes and disomes, which, unexpectedly, has no obvious impact on animal biology. Because transcripts that are enriched in polysomes in wild-type animals tend to be less abundant in the absence of CEYs, our findings suggest that large polysomes might depend on transcript stabilization mediated by CEY proteins.
Friedrich Miescher Institute for Biomedical Research, Basel 4058, Switzerland University of Basel, Petersplatz 1, CH-4003 Basel, Switzerland.
Andreas
A
Arnold
Department of Biochemistry and Molecular Biology, Monash University, Victoria 3800, Australia.
Md Masuder
MM
Rahman
Department of Biochemistry and Molecular Biology, Monash University, Victoria 3800, Australia.
Man Chun
MC
Lee
Friedrich Miescher Institute for Biomedical Research, Basel 4058, Switzerland.
Sandra
S
Muehlhaeusser
Friedrich Miescher Institute for Biomedical Research, Basel 4058, Switzerland.
Iskra
I
Katic
Friedrich Miescher Institute for Biomedical Research, Basel 4058, Switzerland Swiss Institute of Bioinformatics, CH-4058 Basel, Switzerland.
Dimos
D
Gaidatzis
Friedrich Miescher Institute for Biomedical Research, Basel 4058, Switzerland.
Daniel
D
Hess
Friedrich Miescher Institute for Biomedical Research, Basel 4058, Switzerland University of Basel, Petersplatz 1, CH-4003 Basel, Switzerland.
Claudia
C
Scheckel
Friedrich Miescher Institute for Biomedical Research, Basel 4058, Switzerland.
Jane E
JE
Wright
Department of Neuroscience, Biozentrum/Pharmazentrum, Basel 4046, Switzerland.
Attila
A
Stetak
Department of Biochemistry and Molecular Biology, Monash University, Victoria 3800, Australia.
Peter R
PR
Boag
Friedrich Miescher Institute for Biomedical Research, Basel 4058, Switzerland rafal.ciosk@fmi.ch.
Rafal
R
Ciosk
D000818:Animals; D017173:Caenorhabditis elegans / Q000235:genetics / Q000254:growth & development / Q000378:metabolism; D029742:Caenorhabditis elegans Proteins / Q000032:analysis / Q000502:physiology*; D003593:Cytoplasm / Q000737:chemistry; D011132:Polyribosomes / Q000378:metabolism*; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000032:analysis / Q000502:physiology*; D012261:Ribonucleoproteins / Q000737:chemistry
D029742:Caenorhabditis elegans Proteins; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins; C026452:messenger ribonucleoprotein