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. 2013 Sep-Dec;4(5):217-20.
doi: 10.4161/trns.26594.

Zinc’ing down RNA polymerase I

Guillaume F Chanfreau

Zinc’ing down RNA polymerase I

Guillaume F Chanfreau. Transcription. 2013 Sep-Dec.

Abstract

Most RNA polymerases contain zinc, yet the precise function of zinc and its influence of polymerases stability are unknown. A recent study provides evidence that zinc levels control the stability of RNA polymerase I in vivo and that the enzyme might serve as a zinc reservoir for other proteins.

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Figures

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Figure 1. Shown is the equilibrium between ubiquitinated states of the RNA polymerase I complex, and the consequences of these differences in ubiquitination on the stability of the Polymerase I complex. The identity of the ubiquitin proteases that promote the deubiquitination reactions is indicated. Ubi1 and Ubi2 would correspond to the different ubiquitinated states, which would result in RNAP I degradation and nuclear retention, respectively.
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