Analysis of ubiquitin chain-binding proteins by two-hybrid methods

Jennifer Apodaca, Jungmi Ahn, Ikjin Kim, Hai Rao

Research output: Contribution to journalArticle

Abstract

Ubiquitin (Ub) regulates important cellular processes through covalent attachment to its substrates. Distinct fates are bestowed on multi-Ub chains linked through different lysine residues. Ub contains seven conserved lysines, all of which could be used for multi-Ub chain formation. K29 and K48 are the signals for proteasome-mediated proteolysis. Multi-Ub chains linked through K63 have nonproteolytic functions. Studies of Ub-binding factors are likely the key to understanding diverse functions of the Ub molecule. Yeast two-hybrid assay can be a powerful approach to dissect the interaction between Ub and its binding proteins and also the function of these Ub-chain binding proteins in vivo.

Original languageEnglish (US)
Article number10
Pages (from-to)157-164
Number of pages8
JournalMethods in Enzymology
Volume399
DOIs
StatePublished - 2005

Fingerprint

Two-Hybrid System Techniques
Ubiquitin
Carrier Proteins
Lysine
Proteolysis
Proteasome Endopeptidase Complex
Yeast
Assays
Molecules

ASJC Scopus subject areas

  • Biochemistry

Cite this

Analysis of ubiquitin chain-binding proteins by two-hybrid methods. / Apodaca, Jennifer; Ahn, Jungmi; Kim, Ikjin; Rao, Hai.

In: Methods in Enzymology, Vol. 399, 10, 2005, p. 157-164.

Research output: Contribution to journalArticle

Apodaca, Jennifer ; Ahn, Jungmi ; Kim, Ikjin ; Rao, Hai. / Analysis of ubiquitin chain-binding proteins by two-hybrid methods. In: Methods in Enzymology. 2005 ; Vol. 399. pp. 157-164.
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