Abstract
The intracellular level or activity of proteins can be regulated at numerous levels. In most cells, one of the principal mechanisms employed is the regulation of transcription initiation. Transcription regulators are therefore among the main regulatory proteins in the cell. As such, control of their concentration—as well as their activity—has to be tightly regulated. Rapid modulation of the concentration of a protein requires it to be relatively short-lived. It is not surprising, then, that the half-lives of many transcription factors are well below the average for cellular proteins. Half-lives as low as 1 min have been measured for some bacterial transcription factors, e. g., cII (Gottesman et al., 1981) and σ32 (Strauss et al., 1987). A number of yeast transcription factors are known to have half-lives of only 3–5 min, e. g., Matα2 (Hochstrasser and Varshavsky, 1990) and Gcn4 (Kornitzer et al., 1994). The mammalian transcription factors c-fos (Curran et al., 1984) and c-myc (Luscher and Eisenman, 1988) have half-lives of ∼ 20 min. In eukaryotes, most known cases of rapidly degraded transcription regulators involve the ubiquitin—proteasome pathway. In this chapter, we will review some of the best-studied examples of degradation of transcription factors by this pathway.
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Hochstrasser, M., Kornitzer, D. (1998). Ubiquitin-Dependent Degradation of Transcription Regulators. In: Peters, JM., Harris, J.R., Finley, D. (eds) Ubiquitin and the Biology of the Cell. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1922-9_9
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