Abstract:
:The 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 rpn10delta yeast suggesting that this polyubiquitin binding protein is not required for the rGA effect. The conserved effect of the GA repeat in yeast opens the possibility for the use of genetic screens to unravel its mode of action.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Heessen S,Dantuma NP,Tessarz P,Jellne M,Masucci MGdoi
10.1016/s0014-5793(03)01296-1keywords:
subject
Has Abstractpub_date
2003-12-04 00:00:00pages
397-404issue
2eissn
0014-5793issn
1873-3468pii
S0014579303012961journal_volume
555pub_type
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