AbstractThe glycine-alanine (GA) repeat of the Epstein–Barr virus nuclear antigen-1 inhibits in cis ubiquitin-dependent proteolysis in mammalian cells through a yet unknown mechanism. In the present study we demonstrate that the GA repeat targets an evolutionarily conserved step in proteolysis since it can prevent the degradation of proteasomal substrates in the yeast Saccharomyces cerevisiae. Insertion of yeast codon-optimised recombinant GA (rGA) repeats of different length in green fluorescent protein reporters harbouring N-end rule or ubiquitin fusion degradation signals resulted in efficient stabilisation of these substrates. Protection was also achieved in rpn10Δ yeast suggesting that this polyubiquitin binding protein is not required...
Ubiquitin (Ub) regulates important cellular processes through covalent attachment to its substrates....
AbstractLigation of proteins to ubiquitin requires activation of ubiquitin by E1, the ubiquitin-acti...
AbstractProteolysis by the ubiquitin-proteasome pathway is often regulated, but the mechanisms under...
AbstractThe glycine-alanine (GA) repeat of the Epstein–Barr virus nuclear antigen-1 inhibits in cis ...
The glycine-alanine (GA) repeat of the Epstein-Barr virus nuclear antigen-1 inhibits in cis ubiquiti...
The ubiquitin-proteasome system plays a fundamental role in virtually every cellular process. Degrad...
AbstractThe Gly–Ala repeat (GAr) of the Epstein–Barr virus nuclear antigen 1 is a cis acting inhibit...
The ubiquitin-proteasome pathway plays a central role in the controlled degradation of shortlived an...
AbstractRapid degradation of specific regulatory proteins plays a role in a wide range of cellular p...
Regulated protein destruction by the proteasome is crucial for the maintenance of normal cellular ho...
AbstractA cell-free system has been developed in budding yeast that provides direct evidence that th...
Ubiquitin-dependent proteasomal degradation is of paramount importance for cellular processes such a...
SummaryAll seven lysine residues in ubiquitin contribute to the synthesis of polyubiquitin chains on...
Ubiquitin-dependent proteasomal degradation is of paramount importance for cellular processes such a...
AbstractProteinase yscE, the proteasome/multicatalytic—multifunctional proteinase of yeast had been ...
Ubiquitin (Ub) regulates important cellular processes through covalent attachment to its substrates....
AbstractLigation of proteins to ubiquitin requires activation of ubiquitin by E1, the ubiquitin-acti...
AbstractProteolysis by the ubiquitin-proteasome pathway is often regulated, but the mechanisms under...
AbstractThe glycine-alanine (GA) repeat of the Epstein–Barr virus nuclear antigen-1 inhibits in cis ...
The glycine-alanine (GA) repeat of the Epstein-Barr virus nuclear antigen-1 inhibits in cis ubiquiti...
The ubiquitin-proteasome system plays a fundamental role in virtually every cellular process. Degrad...
AbstractThe Gly–Ala repeat (GAr) of the Epstein–Barr virus nuclear antigen 1 is a cis acting inhibit...
The ubiquitin-proteasome pathway plays a central role in the controlled degradation of shortlived an...
AbstractRapid degradation of specific regulatory proteins plays a role in a wide range of cellular p...
Regulated protein destruction by the proteasome is crucial for the maintenance of normal cellular ho...
AbstractA cell-free system has been developed in budding yeast that provides direct evidence that th...
Ubiquitin-dependent proteasomal degradation is of paramount importance for cellular processes such a...
SummaryAll seven lysine residues in ubiquitin contribute to the synthesis of polyubiquitin chains on...
Ubiquitin-dependent proteasomal degradation is of paramount importance for cellular processes such a...
AbstractProteinase yscE, the proteasome/multicatalytic—multifunctional proteinase of yeast had been ...
Ubiquitin (Ub) regulates important cellular processes through covalent attachment to its substrates....
AbstractLigation of proteins to ubiquitin requires activation of ubiquitin by E1, the ubiquitin-acti...
AbstractProteolysis by the ubiquitin-proteasome pathway is often regulated, but the mechanisms under...