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Methods for the purification of ubiquitinated Proteins
Author(s) -
Tomlinson Emma,
Palaniyappan Naaventhan,
Tooth David,
Layfield Robert
Publication year - 2007
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200601008
Subject(s) - ubiquitin , proteasome , posttranslational modification , computational biology , proteomics , protein degradation , proteolysis , chemistry , biochemistry , ubiquitins , f box protein , biology , microbiology and biotechnology , ubiquitin ligase , enzyme , gene
Post‐translational protein modification by the covalent conjugation of ubiquitin, originally implicated as a signal for proteolytic degradation by 26S proteasome, has now been realised to play important roles in the regulation of almost all biological processes in eukaryotes. In order to understand these processes in greater detail there is a requirement for techniques that can purify mixtures of ubiquitin‐conjugated proteins, as a prerequisite to their identification and characterisation. Here we review the methods that have been applied to the bulk purification of ubiquitinated proteins and discuss their applications in proteomic analyses of the ‘ubiquitome’.