A universal strategy for proteomic studies of SUMO and other ubiquitin-like modifiers.

ABSTRACT: Post-translational modification by the conjugation of small ubiquitin-like modifiers is an essential mechanism to affect protein function. Currently, only a limited number of substrates are known for most of these modifiers, thus limiting our knowledge of their role and relevance for cellular physiology. Here, we report the development of a universal strategy for proteomic studies of ubiquitin-like modifiers. This strategy involves the development of stable transfected cell lines expressing a double-tagged modifier under the control of a tightly negatively regulated promoter, the induction of the expression and conjugation of the tagged modifier to cellular proteins, the tandem affinity purification of the pool of proteins covalently modified by the tagged modifier, and the identification

SUBMITTER: Rosas-Acosta G 

PROVIDER: S-EPMC3477800 | biostudies-literature | 2005 Jan

REPOSITORIES: biostudies-literature