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Ubiquitin | Open Access Journals
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Journal of Tissue Science and Engineering

ISSN: 2157-7552

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Ubiquitin

Ubiquitin is a small regulatory protein (8.6 kDa) found in most tissues of eukaryotic organisms, i.e. it is ubiquitous. It was discovered in 1975 by Gideon Goldstein and further characterized in the 1970s and 1980s. Four genes in the human genome code for ubiquitin: UBB, UBC, UBA52 and RPS27A. The addition of ubiquitin to a protein substrate is called ubiquitination (or, more rarely, ubiquitylation or ubiquitinylation). Ubiquitination affects proteins in several ways: it can mark them for degradation via the proteasome, modify their cellular localization, affect their activity and promote or prevent protein interactions. Ubiquitination comprises three main stages: activation, conjugation and ligation , performed by ubiquitin. activation enzymes (E1), ubiquitin conjugation enzymes (E2) and ubiquitin ligases (E3), respectively. The result of this sequential cascade is to bind ubiquitin to the lysine residues on the protein substrate via an isopeptide bond, the cysteine ​​residues via a thioester bond, the serine and threonine residues via an ester bond, or the amino group at the end. N of the protein via a peptide bond.

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