Hartmann-Petersen Rasmus, Hendil Klavs B, Gordon Colin
August Krogh Institute, University of Copenhagen, Universitetsparken 13, DK-2100 Copenhagen O, Denmark.
FEBS Lett. 2003 Jan 30;535(1-3):77-81. doi: 10.1016/s0014-5793(02)03874-7.
As a step in their turnover proteins in eukaryotic cells are coupled to a small protein, ubiquitin, before they are recognised by 26S proteasomes and degraded. However, cells also contain many deubiquitinating enzymes, which can rescue proteins by cleaving off the ubiquitin chains. Here we report that three ubiquitin binding proteins, Rhp23, Dph1 and Pus1, from fission yeast can protect multiubiquitin conjugates against deubiquitination. This protection depends on the ubiquitin binding domains and may promote degradation of ubiquitinated proteins.
在真核细胞中,蛋白质在被26S蛋白酶体识别并降解之前,其周转过程的一个步骤是与一种小蛋白泛素结合。然而,细胞中也含有许多去泛素化酶,它们可以通过切断泛素链来拯救蛋白质。在此我们报告,来自裂殖酵母的三种泛素结合蛋白Rhp23、Dph1和Pus1可以保护多泛素缀合物不被去泛素化。这种保护作用依赖于泛素结合结构域,并且可能促进泛素化蛋白质的降解。