Journal
PLOS ONE
Volume 11, Issue 5, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0156365
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Funding
- Protein Science Translation Core, part of the South Carolina Lipidomics and Pathology Center of Biomedical Research Excellence, National Institutes of Health Grant [MUCR-2211000-89623-2021-02]
- American Cancer Society Institutional Research Grant [IRG-97-219-11]
- National Institutes of Health/National Cancer Institute, NIH/NCI [1R01CA172567-01A1]
- National Institutes of Health/National Institute of Neurological Disorders and Stroke [1R01-NS041596]
- Natural Sciences and Engineering Research Council of Canada
- Canadian Government through a Genome Canada grant
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The RNA-binding protein La is involved in several aspects of RNA metabolism including the translational regulation of mRNAs and processing of pre-tRNAs. Besides its well-described phosphorylation by Casein kinase 2, the La protein is also posttranslationally modified by the Small Ubiquitin-like MOdifier (SUMO), but the functional outcome of this modification has not been defined. The objective of this study was to test whether sumoylation changes the RNA-binding activity of La. Therefore, we established an in vitro sumoylation assay for recombinant human La and analyzed its RNA-binding activity by electrophoretic mobility shift assays. We identified two novel SUMO-acceptor sites within the La protein located between the RNA recognition motif 1 and 2 and we demonstrate for the first time that sumoylation facilitates the RNA-binding of La to small RNA oligonucleotides representing the oligopyrimidine tract (TOP) elements from the 5' untranslated regions (UTR) of mRNAs encoding ribosomal protein L22 and L37 and to a longer RNA element from the 5' UTR of cyclin D1 (CCND1) mRNA in vitro. Furthermore, we show by RNA immunoprecipitation experiments that a La mutant deficient in sumoylation has impaired RNA-binding activity in cells. These data suggest that modulating the RNA-binding activity of La by sumoylation has important consequences on its functionality.
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