The recruitment of RNA polymerase I on rDNA is mediated by the interaction of the A43 subunit with Rrn3

Autor: Patrick Schultz, Christophe Carles, Gérald Peyroche, Herbert Tschochner, Nicolas Bischler, André Sentenac, Michel Riva, Philipp Milkereit
Přispěvatelé: CEA- Saclay (CEA), Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Universität Heidelberg [Heidelberg] = Heidelberg University, Institut de génétique et biologie moléculaire et cellulaire (IGBMC), Université Louis Pasteur - Strasbourg I-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)
Rok vydání: 2000
Předmět:
Models
Molecular
Saccharomyces cerevisiae Proteins
Transcription
Genetic
Macromolecular Substances
Protein subunit
Molecular Sequence Data
Saccharomyces cerevisiae
Biology
DNA
Ribosomal
General Biochemistry
Genetics and Molecular Biology
Fungal Proteins
RNA Polymerase I
Transcription (biology)
Gene Expression Regulation
Fungal
Two-Hybrid System Techniques
Image Processing
Computer-Assisted
RNA polymerase I
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
Amino Acid Sequence
DNA
Fungal
Promoter Regions
Genetic
Molecular Biology
Ribosomal DNA
Transcription factor
Genetics
Binding Sites
General Immunology and Microbiology
General Neuroscience
RNA
Epistasis
Genetic
Promoter
Articles
Recombinant Proteins
Microscopy
Electron
Protein Subunits
Pol1 Transcription Initiation Complex Proteins
Mutation
Sequence Alignment
Protein Binding
Transcription Factors
Zdroj: EMBO Journal
EMBO Journal, 2000, 19 (20), pp.5473-5482. ⟨10.1093/emboj/19.20.5473⟩
ISSN: 1460-2075
0261-4189
Popis: RNA polymerase I (Pol I) is dedicated to transcription of the large ribosomal DNA (rDNA). The mechanism of Pol I recruitment onto rDNA promoters is poorly understood. Here we present evidence that subunit A43 of Pol I interacts with transcription factor Rrn3: conditional mutations in A43 were found to disrupt the transcriptionally competent Pol I-Rrn3 complex, the two proteins formed a stable complex when co-expressed in Escherichia coli, overexpression of Rrn3 suppressed the mutant phenotype, and A43 and Rrn3 mutants showed synthetic lethality. Consistently, immunoelectron microscopy data showed that A43 and Rrn3 co-localize within the Pol I-Rrn3 complex. Rrn3 has several protein partners: a two-hybrid screen identified the C-terminus of subunit Rrn6 of the core factor as a Rrn3 contact, an interaction supported in vitro by affinity chromatography. Our results suggest that Rrn3 plays a central role in Pol I recruitment to rDNA promoters by bridging the enzyme to the core factor. The existence of mammalian orthologues of A43 and Rrn3 suggests evolutionary conservation of the molecular mechanisms underlying rDNA transcription in eukaryotes.
Databáze: OpenAIRE
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