ArticlePlant molecular biology2001
RNA polymerase I holoenzyme-promoter complexes include an associated CK2-like protein kinase.
Article in Plant molecular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 21 citations in OpenAlex.
- Ribosome Biogenesis in Plants: From Functional 45S Ribosomal DNA Organization to Ribosome Assembly Factors.The Plant cell · 2019Review
- Potential interface between ribosomal protein production and pre-rRNA processing.Molecular and cellular biology · 2007Article
- Casein kinase 2 associates with initiation-competent RNA polymerase I and has multiple roles in ribosomal DNA transcription.Molecular and cellular biology · 2006Article
- CK2-mediated stimulation of Pol I transcription by stabilization of UBF-SL1 interaction.Nucleic acids research · 2006Article
- Arabidopsis kinome: after the casting.Functional & integrative genomics · 2004Review
- Multiple protein-protein interactions by RNA polymerase I-associated factor PAF49 and role of PAF49 in rRNA transcription.Molecular and cellular biology · 2004Article
- Bromodomain factor 1 (Bdf1) is phosphorylated by protein kinase CK2.Molecular and cellular biology · 2004Article
- Transcription and tyranny in the nucleolus: the organization, activation, dominance and repression of ribosomal RNA genes.The arabidopsis book · 2002Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 3 countries.
Funding
Abstract
In eukaryotes, RNA polymerase I (pol I) transcribes the tandemly repeated genes that encode the precursor of 18S, 5.8S and 25S ribosomal RNAs. In plants and animals, the pol I enzyme can be purified in a holoenzyme form that is self-sufficient for promoter binding and accurate, promoter-dependent transcription in a cell-free system. In this report, we show that a casein kinase 2 (CK2)-like protein kinase co-purifies with pol I holoenzyme activity purified from broccoli (Brassica oleracea). Using an immobilized template assay, we show that the CK2-like activity is part of the protein-DNA complex that results upon binding of the holoenzyme to the rRNA gene promoter. The CK2 activity phosphorylates a similar set of holoenzyme proteins both before and after promoter binding. These data provide further evidence that pol I holoenzyme activity can be attributed to a single, multi-protein complex self-sufficient for promoter association and accurate, promoter-dependent transcription.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.