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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

URM1 Urm1p

Urm1, Urm1p
Top mentioned proteins: MOCS3, Ubiquitin, CAN, Thio, Dys
Papers on Urm1
In silico identification of genetically attenuated vaccine candidate genes for Plasmodium liver stage.
Gomes et al., Delhi, India. In Infect Genet Evol, Dec 2015
Among these 310 possible GAP candidates, we further studied Plasmodium liver stage proteins by phyletic distribution and functional domain analyses and shortlisted twenty GAP-candidates; these are: fabB/F, fabI, arp, 3 genes encoding subunits of the PDH complex, dnaJ, urm1, rS5, ancp, mcp, arh, gk, lisp2, valS, palm, and four conserved Plasmodium proteins of unknown function.
Protein degradation and dynamic tRNA thiolation fine-tune translation at elevated temperatures.
Pedrioli et al., Zürich, Switzerland. In Nucleic Acids Res, Jun 2015
The abundance of Ncs2p and Ncs6p, two members of the URM1 pathway responsible for the thiolation of wobble uridines in cytoplasmic tRNAs tK(UUU), tQ(UUG) and tE(UUC), is down-regulated in a proteasomal dependent fashion.
An evolutionary approach uncovers a diverse response of tRNA 2-thiolation to elevated temperatures in yeast.
Leidel et al., Münster, Germany. In Rna, Feb 2015
Our results suggest that loss of 2-thiolation follows accumulation of newly synthesized tRNA that lack s(2)U34 modification due to temperature sensitivity of the URM1 pathway in S. cerevisiae and S. bayanus.
tRNA thiolation links translation to stress responses in Saccharomyces cerevisiae.
Ploegh et al., Cambridge, United States. In Mol Biol Cell, Feb 2015
The URM1 pathway is required for thiolation of the cytoplasmic tRNAs tGlu(UUC), tGln(UUG), and tLys(UUU) in Saccharomyces cerevisiae.
Loss of anticodon wobble uridine modifications affects tRNA(Lys) function and protein levels in Saccharomyces cerevisiae.
Schaffrath et al., Kassel, Germany. In Plos One, 2014
While mutations in subunits of the Elongator complex (Elp1-Elp6), which disable mcm5 side chain formation, or removal of components of the thiolation pathway (Ncs2/Ncs6, Urm1, Uba4) are individually tolerated, the combination of both modification defects has been reported to have lethal effects on Saccharomyces cerevisiae.
tRNA tKUUU, tQUUG, and tEUUC wobble position modifications fine-tune protein translation by promoting ribosome A-site binding.
Pedrioli et al., Zürich, Switzerland. In Proc Natl Acad Sci U S A, 2013
In eukaryotes, the URM1 and ELP pathways increase cellular resistance to various stress conditions, such as nutrient starvation and oxidative agents, by promoting thiolation and methoxycarbonylmethylation, respectively, of the wobble uridine of cytoplasmic (tK(UUU)), (tQ(UUG)), and (tE(UUC)).
Dual role of the molybdenum cofactor biosynthesis protein MOCS3 in tRNA thiolation and molybdenum cofactor biosynthesis in humans.
Leimkühler et al., Potsdam, Germany. In J Biol Chem, 2012
We showed that MOCS3 activates both MOCS2A and URM1 by adenylation and a subsequent sulfur transfer step for the formation of the thiocarboxylate group at the C terminus of each protein.
Modification by ubiquitin-like proteins: significance in apoptosis and autophagy pathways.
Ntwasa et al., Johannesburg, South Africa. In Int J Mol Sci, 2011
Modifiers such as SUMO, ATG12, ISG15, FAT10, URM1, and UFM have been shown to modify proteins thus conferring functions related to programmed cell death, autophagy and regulation of the immune system.
Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-directed protein modifier.
Jentsch et al., Cambridge, United States. In Proc Natl Acad Sci U S A, 2011
Urm1 has a conserved dual role by integrating the functions of prokaryotic sulfur carriers with those of eukaryotic protein modifiers of the Ub family
Urm1 couples sulfur transfer to ubiquitin-like protein function in oxidative stress.
Wolf et al., Los Angeles, United States. In Proc Natl Acad Sci U S A, 2011
observations suggest that Urm1 activation is more similar to that of a prokaryotic sulfur carrier protein than that of a ubiquitin-like protein
Allele-specific suppressors of lin-1(R175Opal) identify functions of MOC-3 and DPH-3 in tRNA modification complexes in Caenorhabditis elegans.
Han et al., Boulder, United States. In Genetics, 2010
In yeast, the ELP complex has been shown to genetically interact with Uba4p/Urm1p and Kti11-13p for a function in tRNA modification.
Archaeal ubiquitin-like proteins: functional versatility and putative ancestral involvement in tRNA modification revealed by comparative genomic analysis.
Koonin et al., Bethesda, United States. In Archaea, 2009
Therefore it is hypothesized that the ancestral function of the archaeal Ubl proteins is sulfur insertion into modified nucleotides in tRNAs, an activity analogous to that of the URM1 protein in eukaryotes.
Genetic polymorphisms and preliminary association analysis with production traits of the porcine SLC27A4 gene.
Zuo et al., Wuhan, China. In Mol Biol Rep, 2009
In silico mapping assigned SLC27A4 gene between gene COQ4 (coenzyme Q4 homolog) and URM1 (ubiquitin related modifier 1 homolog) on pig chromosome 1q24-q2.12
Ubiquitin-related modifier Urm1 acts as a sulphur carrier in thiolation of eukaryotic transfer RNA.
Peter et al., Zürich, Switzerland. In Nature, 2009
Urm1p, the most ancient UBL, acts as a sulphur carrier in the process of eukaryotic transfer RNA (tRNA) modification, providing a possible evolutionary link between Ubiquitin-like proteins and sulphur transfer
Mechanistic characterization of the sulfur-relay system for eukaryotic 2-thiouridine biogenesis at tRNA wobble positions.
Suzuki et al., Tokyo, Japan. In Nucleic Acids Res, 2009
We have identified five genes in Saccharomyces cerevisiae, YIL008w (URM1), YHR111w (UBA4), YOR251c (TUM1), YNL119w (NCS2) and YGL211w (NCS6), that are required for 2-thiolation of mcm(5)s(2)U.
A functional proteomics approach links the ubiquitin-related modifier Urm1 to a tRNA modification pathway.
Ploegh et al., Cambridge, United States. In Proc Natl Acad Sci U S A, 2008
Urm1 is activated by an unusual mechanism to yield a thiocarboxylate intermediate that serves as sulfur donor in tRNA thiolation reactions
Thio-modification of yeast cytosolic tRNA requires a ubiquitin-related system that resembles bacterial sulfur transfer systems.
Hayashi et al., Takatsuki, Japan. In J Biol Chem, 2008
ubiquitin-like protein Urm1 and ubiquitin-activating enzyme-like protein Uba4, as well as Tuc1 and Tuc2, were strictly required for tRNA thio-modification
A genome-wide screen identifies genes required for formation of the wobble nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces cerevisiae.
Byström et al., Umeå, Sweden. In Rna, 2008
In addition to earlier described mutants, formation of the s(2) group was also abolished in urm1, uba4, and ncs2 mutants and decreased in the yor251c mutant.
Attachment of the ubiquitin-related protein Urm1p to the antioxidant protein Ahp1p.
Sprague et al., Eugene, United States. In Eukaryot Cell, 2003
Urm1p is a ubiquitin-related protein that serves as a posttranslational modification of other proteins.
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