Inhibition of ubiquitin/proteasome-dependent proteolysis in Saccharomyces cerevisiae by a Gly-Ala repeat.

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 Lett

journal_title

FEBS letters

authors

Heessen S,Dantuma NP,Tessarz P,Jellne M,Masucci MG

doi

10.1016/s0014-5793(03)01296-1

keywords:

subject

Has Abstract

pub_date

2003-12-04 00:00:00

pages

397-404

issue

2

eissn

0014-5793

issn

1873-3468

pii

S0014579303012961

journal_volume

555

pub_type

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