Glycolytic enzymes localize to ribonucleoprotein granules in Drosophila germ cells, bind Tudor and protect from transposable elements
Authors
Gao, MingThomson, Travis
Creed, T Michael
Tu, Shikui
Loganathan, Sudan N.
Jackson, Christina A.
McCluskey, Patrick
Lin, Yanyan
Collier, Scott E.
Weng, Zhiping
Lasko, Paul
Ohi, Melanie D.
Arkov, Alexey L.
UMass Chan Affiliations
Program in Molecular MedicineProgram in Bioinformatics and Integrative Biology
Document Type
Journal ArticlePublication Date
2015-03-01Keywords
Biochemistry, Biophysics, and Structural BiologyBioinformatics
Computational Biology
Integrative Biology
Systems Biology
Metadata
Show full item recordAbstract
Germ cells give rise to all cell lineages in the next-generation and are responsible for the continuity of life. In a variety of organisms, germ cells and stem cells contain large ribonucleoprotein granules. Although these particles were discovered more than 100 years ago, their assembly and functions are not well understood. Here we report that glycolytic enzymes are components of these granules in Drosophila germ cells and both their mRNAs and the enzymes themselves are enriched in germ cells. We show that these enzymes are specifically required for germ cell development and that they protect their genomes from transposable elements, providing the first link between metabolism and transposon silencing. We further demonstrate that in the granules, glycolytic enzymes associate with the evolutionarily conserved Tudor protein. Our biochemical and single-particle EM structural analyses of purified Tudor show a flexible molecule and suggest a mechanism for the recruitment of glycolytic enzymes to the granules. Our data indicate that germ cells, similarly to stem cells and tumor cells, might prefer to produce energy through the glycolytic pathway, thus linking a particular metabolism to pluripotency.Source
EMBO Rep. 2015 Mar;16(3):379-86. doi: 10.15252/embr.201439694. Epub 2015 Jan 18. Link to article on publisher's siteDOI
10.15252/embr.201439694Permanent Link to this Item
http://hdl.handle.net/20.500.14038/25905PubMed ID
25600116Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.15252/embr.201439694