title: Fructose bisphosphate aldolase is involved in the control of RNA polymerase III-directed transcription.
abstract: 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 C128 protein, the second largest subunit of the RNA polymerase III complex. The suppression of the growth phenotype by Fba1 is accompanied by enhanced de novo tRNA transcription in rpc128-1007 cells. We inactivated residues critical for the catalytic activity of Fba1. 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 Fba1 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 III transcription and aldolase.
authors.affiliation: Institute of Biochemistry and Biophysics, Polish Academy of Sciences, ul. Pawinskiego 5a, 02-106 Warsaw, Poland.
authors.forename: Małgorzata
authors.initials: M
authors.lastname: Cieśla
authors.affiliation: Institute of Biotechnology, Faculty of Chemistry, Warsaw University of Technology, ul. Noakowskiego 3, 00-664 Warsaw, Poland.
authors.forename: Jolanta
authors.initials: J
authors.lastname: Mierzejewska
authors.affiliation: Institute of Biotechnology, Faculty of Chemistry, Warsaw University of Technology, ul. Noakowskiego 3, 00-664 Warsaw, Poland.
authors.forename: Małgorzata
authors.initials: M
authors.lastname: Adamczyk
authors.affiliation: Department of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, SE 106 91 Stockholm, Sweden.
authors.forename: Ann-Kristin Östlund
authors.initials: AK
authors.lastname: Farrants
authors.affiliation: Institute of Biochemistry and Biophysics, Polish Academy of Sciences, ul. Pawinskiego 5a, 02-106 Warsaw, Poland; Institute of Biotechnology, Faculty of Chemistry, Warsaw University of Technology, ul. Noakowskiego 3, 00-664 Warsaw, Poland. Electronic address: magda@ibb.waw.pl.
authors.forename: Magdalena
authors.initials: M
authors.lastname: Boguta
mesh_terms: D015152:Blotting, Northern; D015153:Blotting, Western; D002467:Cell Nucleus / Q000378:metabolism; D002843:Chromatin / Q000235:genetics; D047369:Chromatin Immunoprecipitation; D003593:Cytoplasm / Q000378:metabolism; D005455:Fluorescent Antibody Technique; D005634:Fructose-Bisphosphate Aldolase / Q000235:genetics / Q000378:metabolism*; D047468:Immunoprecipitation; D016297:Mutagenesis, Site-Directed; D009154:Mutation / Q000235:genetics; D012320:RNA Polymerase III / Q000235:genetics / Q000378:metabolism*; D012333:RNA, Messenger / Q000235:genetics; D012343:RNA, Transfer / Q000235:genetics / Q000378:metabolism*; D060888:Real-Time Polymerase Chain Reaction; D020133:Reverse Transcriptase Polymerase Chain Reaction; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000254:growth & development / Q000378:metabolism; D014158:Transcription, Genetic
chemical_list: D002843:Chromatin; D012333:RNA, Messenger; D012343:RNA, Transfer; D012320:RNA Polymerase III; D005634:Fructose-Bisphosphate Aldolase
keywords: Aldolase; Pol III; Yeast; tRNA transcription