Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1843, Issue 6, Pages 1103-1110Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2014.02.007
Keywords
Aldolase; tRNA transcription; Pol III; Yeast
Categories
Funding
- Foundation for Polish Science [2010-2/2]
- National Science Center, Poland [N301693740, 2012/05/E/NZ2/00583]
- Warsaw University of Technology, Faculty of Chemistry
Ask authors/readers for more resources
Yeast Fba1 (fructose 1,6-bisphosphate aldolase) is a glycolytic enzyme essential for viability. The overproduction of Fba1 enables overcoming of a severe growth defect caused by a missense mutation rpc128-1007 in a gene encoding the 028 protein, the second largest subunit of the RNA polymerase III complex. The suppression of the growth phenotype by Fbal is accompanied by enhanced de novo tRNA transcription in rpc128-1007 cells. We inactivated residues critical for the catalytic activity of Fbal. Overproduction of inactive aldolase still suppressed the rpc128-1007 phenotype, indicating that the function of this glycolytic enzyme in RNA polymerase III transcription is independent of its catalytic activity. Yeast Fbal was determined to interact with the RNA polymerase III complex by coimmunoprecipitation. Additionally, a role of aldolase in control of tRNA transcription was confirmed by ChIP experiments. The results indicate a novel direct relationship between RNA polymerase HI transcription and aldolase. (C) 2014 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available