Background Protein ubiquitination is a ubiquitous mechanism in eukaryotes. In Arabidopsis,
ubiquitin modification is mainly mediated by two ubiquitin activating enzymes (E1s), 37 …

Protein ubiquitination requires the concerted action of three enzymes: ubiquitin‐activating
enzyme (E1), ubiquitin‐conjugating enzyme (E2) and ubiquitin ligase (E3). These …

Attachment of ubiquitin to substrate proteins is catalyzed by the three enzymes E1, E2
(ubiquitin conjugating [UBC]), and E3 (ubiquitin ligase). Forty-one functional proteins with a …

Background Ubiquitination is mediated by the sequential action of at least three enzymes:
the E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme) and E3 (ubiquitin …

Most research in the field of ubiquitination has focused on E3 ubiquitin ligases because they
are the specificity determinants of the ubiquitination process. Nevertheless, E2s are …

E3 ubiquitin ligases of the ubiquitin proteasome system (UPS) mediate recognition of
substrates and later transfer the ubiquitin (Ub). They are the most expanded components of …

The protein ubiquitin is a covalent modifier of proteins, including itself. The ubiquitin system
encompasses the enzymes required for catalysing attachment of ubiquitin to substrates as …

Ubiquitination modulates nearly all aspects of plant life. Here, we reconstituted the
Arabidopsis thaliana ubiquitination cascade in Escherichia coli using a synthetic biology …

Since its discovery in the late 1970s, the ubiquitin proteasome pathway appears to be
omnipresent in many research fields. Although originally discovered in animals, the pathway …

Ubiquitin ligases play a central role in determining the specificity of the ubiquitination system
by selecting a myriad of appropriate candidate proteins for modification. The U-box is a …