A non-proteolytic function of ubiquitin in transcription repression

Authors:

Ada Ndoja and Tingting Yao

doi: 10.15698/mic2014.07.159
Volume 1, pp. 253 to 255, published 07/07/2014.

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Affiliations:

Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523, USA.

Keywords: 

transcription, ubiquitination, transcription activator, Cdc48, transcription repression, Met4, R-Smads.

Corresponding Author(s):

Tingting Yao, Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523, USA. Tingting.Yao@ColoState.edu

Conflict of interest statement:

The authors declare that they have no conflict of interest.

Please cite this article as:

Ada Ndoja and Tingting Yao (2014). A non-proteolytic function of ubiquitin in transcription repression. Microbial Cell 1(7): 253-255.

© 2014 Ndoja and Yao. This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduction in any medium, provided the original author and source are acknowledged.

Abstract:

Regulation of transcription is vitally important for maintaining normal cellular homeostasis and is also the basis for cellular differentiation, morphogenesis and the adaptability of any organism. Transcription activators, which orchestrate time and locus-specific assembly of complex transcription machinery, act as key players in these processes. One way in which these activators are controlled is by the covalent attachment of the conserved protein, ubiquitin (Ub), which can serve as either a proteolytic or non-proteolytic signal. For a subset of the activators, polyubiquitination-dependent degradation of the activator controls its abundance. In these cases transcription activation can require protein synthesis as well as internal or external stimulus. In contrast, other activators have been reported to undergo mono- or oligoubiquitination that does not lead to protein degradation. The mechanisms by which monoubiquitination of transcription activators affect their activities have been poorly understood. In a recent study, we demonstrated that monoubiquitination of some transcription activators can inhibit transcription by recruiting the AAA+ ATPase Cdc48 (also known in metazoan organisms as p97 or valosin-contain protein, VCP), which then extracts the ubiquitinated activator from DNA.