2012, Number 2
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TIP Rev Esp Cienc Quim Biol 2012; 15 (2)
La ubiquitinación: un sistema de regulación dinámico de los organismos
Zamudio-Arroyo JM, Peña-Rangel MT, Riesgo-Escovar JR
Language: Spanish
References: 67
Page: 133-141
PDF size: 139.57 Kb.
ABSTRACT
Regulation of genetic expression occurs at different levels, from transcriptional control to post-translational
modification of proteins. Ubiquitination is one such late process, where target proteins are labeled covalently
on a lysine residue with one or more ubiquitin moieties. Ubiquitin itself is a small protein. This mechanism is
evolutionarily conserved, present to some degree in bacteria. In eukaryotes, it is organized around three
conserved enzymes: E1, an activation enzyme, E2 a conjugation enzyme, and E3, a ligation enzyme. This last
class is by far the most diverse, being the main one conferring specificity by guiding E2-ubiquitin complexes
to appropriate targets. Depending on the activation domain they possess, there are three classes of E3 enzymes:
RING-finger, HECT, and U-box. Ubiquitination can signal different outcomes, yet the most studied one is protein
degradation via the 26S proteasome. Studying ubiquitination in whole organisms, especially genetic model
organisms, confers many advantages, chief among them being the possibility of recording responses of
neighboring groups of cells, whether directly affected or not, by the process.
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