Sudestada1, a Drosophila ribosomal prolyl-hydroxylase required for mRNA translation, cell homeostasis, and organ growth.

Journal article

Genome sequences predict the presence of many 2-oxoglutarate (2OG)-dependent oxygenases of unknown biochemical and biological functions in Drosophila. Ribosomal protein hydroxylation is emerging as an important 2OG oxygenase catalyzed pathway, but its biological functions are unclear. We report investigations on the function of Sudestada1 (Sud1), a Drosophila ribosomal oxygenase. As with its human and yeast homologs, OGFOD1 and Tpa1p, respectively, we identified Sud1 to catalyze prolyl-hydrox...

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Authors: Katz, M; Acevedo, J; Loenarz, C; Galagovsky, D; Liu-Yi, P

• Publication status: Published
• Publisher: National Academy of Sciences
• Journal: Proceedings of the National Academy of Sciences of the United States of America
• Volume: 111
• Issue: 11
• Pages: 4025-4030
• Publication date: 2014-03-01
• DOI: 10.1073/pnas.1314485111
• EISSN: 1091-6490
• ISSN: 0027-8424
• Language: English
• Keywords: Body Weights and Measures; Blotting, Western; RNA Interference; Autophagy; Protein Biosynthesis; Chromatography, Liquid; Unfolded Protein Response; DNA Primers; Fat Body; Female; Protein Processing, Post-Translational; Drosophila Proteins; Prolyl Hydroxylases; Homeostasis; Hydroxylation; Tandem Mass Spectrometry; Ribosomal Proteins; Animals; Real-Time Polymerase Chain Reaction; Drosophila; Apoptosis; Animals, Genetically Modified; Gene Knockdown Techniques