Jump to main content
Jump to site search

Issue 5-6, 2005
Previous Article Next Article

Identification of Gal4 activation domain-binding proteins in the 26S proteasome by periodate-triggered cross-linking

Author affiliations

Abstract

A common occurrence in biology is that a regulatory peptide, protein, or small molecule regulates the activity of a large multi-protein complex through direct interactions with a protein(s) in that complex. To characterize the direct receptor of the regulatory molecule, one would ideally like to study the native system. We report here that periodate-triggered cross-linking of catechol-containing regulatory factors, followed by two-dimensional electrophoresis and Western blotting, is an effective method for the characterization of regulatory factor–protein interactions in the context of large multi-protein complexes. We demonstrate the utility of this methodology by identifying the Rpt6/Sug1 and Rpt4/Sug2 proteins as the direct targets of transcriptional activation domains in the 26S proteasome.

Graphical abstract: Identification of Gal4 activation domain-binding proteins in the 26S proteasome by periodate-triggered cross-linking

Back to tab navigation

Publication details

The article was received on 14 Jul 2005, accepted on 15 Sep 2005 and first published on 30 Sep 2005


Article type: Paper
DOI: 10.1039/B510019D
Citation: Mol. BioSyst., 2005,1, 366-372
  •   Request permissions

    Identification of Gal4 activation domain-binding proteins in the 26S proteasome by periodate-triggered cross-linking

    C. T. Archer, L. Burdine and T. Kodadek, Mol. BioSyst., 2005, 1, 366
    DOI: 10.1039/B510019D

Search articles by author

Spotlight

Advertisements