Search results for "Protein urmylation"

showing 3 items of 3 documents

Sulfur transfer and activation by ubiquitin-like modifier system Uba4•Urm1 link protein urmylation and tRNA thiolation in yeast.

2017

Urm1 is a unique dual-function member of the ubiquitin protein family and conserved from yeast to man. It acts both as a protein modifier in ubiquitin-like urmylation and as a sulfur donor for tRNA thiolation, which in concert with the Elongator pathway forms 5-methoxy-carbonyl-methyl-2-thio (mcm5s2) modified wobble uridines (U34) in anticodons. Using Saccharomyces cerevisiae as a model to study a relationship between these two functions, we examined whether cultivation temperature and sulfur supply previously implicated in the tRNA thiolation branch of the URM1 pathway also contribute to proper urmylation. Monitoring Urm1 conjugation, we found urmylation of the peroxiredoxin Ahp1 is suppre…

lcsh:Biology (General)protein urmylationApplied MicrobiologyGeneticstRNase zymocintRNA thiolationE1-like enzyme Uba4Saccharomyces cerevisiaeubiquitin-like modifier Urm1lcsh:QH301-705.5MicrobiologyMolecular Biologysulfur transferase Tum1Microbial cell (Graz, Austria)
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2016

Urm1 is a unique dual-function member of the ubiquitin protein family and conserved from yeast to man. It acts both as a protein modifier in ubiquitin-like urmylation and as a sulfur donor for tRNA thiolation, which in concert with the Elongator pathway forms 5-methoxy-carbonyl-methyl-2-thio (mcm5s2) modified wobble uridines (U34) in anticodons. Using Saccharomyces cerevisiae as a model to study a relationship between these two functions, we examined whether cultivation temperature and sulfur supply previously implicated in the tRNA thiolation branch of the URM1 pathway also contribute to proper urmylation. Monitoring Urm1 conjugation, we found urmylation of the peroxiredoxin Ahp1 is suppre…

0301 basic medicineTRNA modificationbiologyProtein familySaccharomyces cerevisiaeCell Biologybiology.organism_classificationBiochemistry Genetics and Molecular Biology (miscellaneous)MicrobiologyApplied Microbiology and Biotechnology03 medical and health sciences030104 developmental biologyUbiquitinBiochemistryVirologyTransfer RNAGeneticsbiology.proteinParasitologySite-directed mutagenesisPeroxiredoxinMolecular BiologyProtein urmylationMicrobial Cell
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Urmylation and tRNA thiolation functions of ubiquitin-like Uba4·Urm1 systems are conserved from yeast to man

2015

AbstractThe ubiquitin-like protein Urm1 from budding yeast and its E1-like activator Uba4 have dual roles in protein urmylation and tRNA thiolation pathways. To study whether these are conserved among eukaryotes, we used gene shuffles to replace the yeast proteins by their human counterparts, hURM1 and hUBA4/MOCS3. As judged from biochemical and genetical assays, hURM1 and hUBA4 are functional in yeast, albeit at reduced efficiencies. They mediate urmylation of the peroxiredoxin Ahp1, a known urmylation target in yeast, and support tRNA thiolation. Similar to hUBA4, yeast Uba4 itself is modified by Urm1 and hURM1 suggesting target overlap between eukaryal urmylation pathways. In sum, our st…

Saccharomyces cerevisiae ProteinsUba4 (hUBA4/MOCS3)Saccharomyces cerevisiaeBiophysicstRNA thiolationSaccharomyces cerevisiaeBiochemistryUbiquitin-like urmylationRNA TransferUbiquitinStructural BiologyAnticodonGeneticsHumansUbiquitinsMolecular BiologyProtein urmylationGeneUrm1 (hURM1)Conserved SequenceSequence Homology Amino AcidbiologyActivator (genetics)TRNA thiolationCell Biologybiology.organism_classificationNucleotidyltransferasesYeastBiochemistrySulfurtransferasesbiology.proteinPeroxiredoxinHeLa CellsFEBS Letters
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