Eukaryotic transcription is one of the most complex cellular processes and constitutes the first step in protein synthesis. Ubiquitination and subsequent degradation by the 26 S proteasome, on the other hand, represents the final chapter in the life of a protein. Intriguingly, ubiquitin and the ubiquitin– proteasome system play vital roles in the regulation of transcription. Ubiquitin has dual modus operandi: firstly, ubiquitin functions via the 26 S proteasome — it is tagged to components of the transcription machinery, marking them for degradation via the proteasome, which results in the proper exchange of complexes during transcription and the prompt removal of activators after each round of transcription; and secondly, ubiquitin can function independently of the proteasome — histone ubiquitination results in heterochromatin relaxation and assembly of transcription complexes on the promoter, and ubiquitination of transcription factors enhances their transcriptional-activation function. Although ubiquitin and the ubiquitin–proteasome system were initially perceived as a graveyard for proteins, recent advances in molecular biological techniques have redefined their role as a regulatory system that influences the fate of many cellular processes, such as apoptosis, transcription and cell cycle progression.
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Review Article| October 01 2005
Ubiquitin and control of transcription
Sarath C. Dhananjayan ;
Ayesha Ismail ;
1Department of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, 1580 NW 10 Avenue, Miami, FL 33136, U.S.A.
1To whom correspondence should be addressed (email firstname.lastname@example.org).
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Essays Biochem (2005) 41: 69–80.
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John Mayer, Robert Layfield, Sarath C. Dhananjayan, Ayesha Ismail, Zafar Nawaz; Ubiquitin and control of transcription. Essays Biochem 1 October 2005; 41 69–80. doi: https://doi.org/10.1042/bse0410069
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