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Chemoenzymatic Ubiquitination of Artificial Substrates
Author(s) -
Burchak Olga N.,
Jaquinod Michel,
Cottin Claire,
Mugherli Laurent,
Iwai Kazuhiro,
Chatelain François,
Balakirev Maxim Y.
Publication year - 2006
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200600283
Subject(s) - ubiquitin , chemistry , ubiquitins , cysteine , biochemistry , ubiquitin protein ligases , computational biology , ubiquitin ligase , biology , enzyme , gene
Probing an alternative route . Ubiquitin and Ub‐like proteins (Ubl) are attached to cellular proteins through a conserved conjugation pathway. We demonstrate here that Ub and Ubl thioesters, the key intermediates of this pathway, can be readily transferred onto cysteine‐containing artificial substrates. This finding provides new insight into the chemistry of Ub (Ubl) conjugation and can be used for creating different protein probes and microarrays.