Open AccessPupylation versus ubiquitylation: tagging for proteasome‐dependent degradation
Author(s) -
Burns Kristin E.,
Darwin K. Heran
Publication year - 2010
Publication title -
cellular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.542
H-Index - 138
eISSN - 1462-5822
pISSN - 1462-5814
DOI - 10.1111/j.1462-5822.2010.01447.x
Subject(s) - ubiquitin , proteolysis , proteasome , biology , microbiology and biotechnology , protein degradation , computational biology , ubiquitins , pathogen , deubiquitinating enzyme , ubiquitin ligase , biochemistry , enzyme , gene
Summary P rokaryotic u biquitin‐like p rotein (Pup) is the first identified prokaryotic protein that is functionally analogous to ubiquitin. Despite using the proteasome as the end‐point for proteolysis, Pup differs from ubiquitin both biochemically and structurally. We will discuss these differences that have been highlighted by several recent studies. Finally, we will speculate on the possible interactions between the two analogous pathways in pathogen and host.