Ubiquitin, a small protein consisting of 76 amino acids, has been found in all eukaryotic cells studied. It is one of the most conserved proteins known. Ubiquitin is required for ATP-dependent, nonlysosomal intracellular protein degradation, which eliminates most intracellular defective proteins as well as normal proteins with a rapid turnover. Degradation involves covalent binding of ubiquitin to the protein to be degraded and it is believed that in this way ubiquitin acts to label the protein for disposal by intracellular proteases. The most abundant ubiquitin-protein conjugate, however, is ubiquitin-histone H2A. This conjugate is not degraded. Since such ubiquitinated histones are present primarily in actively transcribed chromosomal regions, ubiquitin may play a role in regulation of gene expression.
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