☆ 4.8 Article

RNA Polymerase I Stability Couples Cellular Growth to Metal Availability

MOLECULAR CELL (2013)

期刊

MOLECULAR CELL

卷 51, 期 1, 页码 105-115

出版社

CELL PRESS

DOI: 10.1016/j.molcel.2013.05.005

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Biochemistry & Molecular Biology Cell Biology

资金

Ruth L. Kirschstein National Research Service Award [GM07185]
UCLA Dissertation Year Fellowship
UCLA Chemistry-Biology Interface training program
American Heart Association Western States Affiliate
NIH [GM061518, GM089778]

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Zinc is an essential cofactor of all major eukaryotic RNA polymerases. How the activity of these enzymes is coordinated or regulated according to cellular zinc levels is largely unknown. Here we show that the stability of RNA polymerase I (RNAPI) is tightly coupled to zinc availability in vivo. In zinc deficiency, RNAPI is specifically degraded by proteolysis in the vacuole in a pathway dependent on the exportin Xpo1p and deubiquitination of the RNAPI large subunit Rpa-190p by Ubp2p and Ubp4p. RNAPII is unaffected, which allows for the expression of genes required in zinc deficiency. RNAPI export to the vacuole is required for survival during zinc starvation, suggesting that degradation of zinc-binding subunits might provide a last resort zinc reservoir. These results reveal a hierarchy of cellular transcriptional activities during zinc starvation and show that degradation of the most active cellular transcriptional machinery couples cellular growth and proliferation to zinc availability.

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