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Dissertation
Charakterisierung des Ubiquitin-ähnlichen Proteins Urm1 in Saccharomyces cerevisiae
(2016-05-11)
Das ursprünglich in S. cerevisiae identifizierte Urm1 stellt aufgrund seiner dualen Funktionsweise ein besonderes UBL dar. In einem Prozess, der als Urmylierung bezeichnet wird, kann es ähnlich dem Ubiquitin kovalent mit anderen Proteinen verknüpft werden. Zusätzlich fungiert es aber auch als Schwefelträger, der an der Thiolierung des wobble-Uridins bestimmter cytoplasmatischer tRNAs beteiligt ist. Während neuere Untersuchungen zeigen, dass die Urm1-abhängige tRNA-Thiolierung zu einer effizienten Translation in ...
Aufsatz
Loss of Anticodon Wobble Uridine Modifications Affects tRNALys Function and Protein Levels in Saccharomyces cerevisiae
(2015)
In eukaryotes, wobble uridines in the anticodons of tRNALysUUU, tRNAGluUUC and tRNAGlnUUG are modified to 5-methoxy-carbonyl-methyl-2-thio-uridine (mcm5s2U). 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. Contrary to such absolute requirement ...
Aufsatz
Sulfur transfer and activation by ubiquitin-like modifier system Uba4•Urm1 link protein urmylation and tRNA thiolation in yeast
(2016-10-24)
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 ...
Aufsatz
Loss of wobble uridine modification in tRNA anticodons interferes with TOR pathway signaling
(2014)
Previous work in yeast has suggested that modification of tRNAs, in particular uridine bases in the anticodon wobble position (U34), is linked to TOR (target of rapamycin) signaling. Hence, U34 modification mutants were found to be hypersensitive to TOR inhibition by rapamycin. To study whether this involves inappropriate TOR signaling, we examined interaction between mutations in TOR pathway genes (tip41Δ, sap190Δ, ppm1Δ, rrd1Δ) and U34 modification defects (elp3Δ, kti12Δ, urm1Δ, ncs2Δ) and found the rapamycin ...
Dissertation
Functional analyses of Dph1•Dph2 in synthesis of diphthamide, a clinically relevant modification on eEF2
(2024)
Diphthamide is a unique post-translational modification of a conserved histidine on the eukaryotic translation elongation factor 2 (eEF2). During translation elongation, eEF2 induces translocation of codon-anticodon duplexes across the ribosomal decoding center. Diphthamide is involved in fine-tuning of this process by stabilizing the codon-anticodon duplex and maintaining reading frame accuracy. Initially, diphthamide was identified as the target for diphtheria toxin, enabling ADP-ribosylation of eEF2 and resulting ...