Redox requirements for ubiquitin-like urmylation of Ahp1, a 2-Cys peroxiredoxin from yeast
نویسندگان
چکیده
منابع مشابه
Urmylation and tRNA thiolation functions of ubiquitin-like Uba4·Urm1 systems are conserved from yeast to man.
The 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...
متن کاملSulfur transfer and activation by ubiquitin-like modifier system Uba4•Urm1 link protein urmylation and tRNA thiolation in yeast
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 stud...
متن کاملUrmylation: a ubiquitin-like pathway that functions during invasive growth and budding in yeast.
Ubiquitin is a small modifier protein that is conjugated to substrates to target them for degradation. Recently, a surprising number of ubiquitin-like proteins have been identified that also can be attached to proteins. Herein, we identify two molecular functions for the posttranslational protein modifier from Saccharomyces cerevisiae, Urm1p. Simultaneous loss of Urm1p and Cla4p, a p21-activate...
متن کاملReversal of 2-Cys peroxiredoxin oligomerization by sulfiredoxin.
Hydrogen peroxide (H(2)O(2)) regulates the structure and function of 2-Cys peroxiredoxins (Prxs). Upon oxidation by excess H(2)O(2), Prxs become overoxidized to a sulfinic acid of its peroxidatic cysteine residue, resulting in a structural change from a small oligomer with peroxidase function to a large oligomer with chaperone function. Then, sulfiredoxin (Srx) reduces the overoxidized Prxs by ...
متن کاملDeglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin.
Reversible protein glutathionylation plays a key role in cellular regulation and cell signaling and protects protein thiols from hyperoxidation. Sulfiredoxin (Srx), an enzyme that catalyzes the reduction of Cys-sulfinic acid derivatives of 2-Cys peroxiredoxins (2-Cys Prxs), has been shown to catalyze the deglutathionylation of actin. We show that deglutathionylation of 2-Cys Prx, a family of pe...
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ژورنال
عنوان ژورنال: Redox Biology
سال: 2020
ISSN: 2213-2317
DOI: 10.1016/j.redox.2020.101438