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dc.contributor.authorRytkönen, Anna K.
dc.contributor.authorHillukkala, Tomi
dc.contributor.authorVaara, Markku
dc.contributor.authorSokka, Miiko
dc.contributor.authorJokela, Maarit
dc.contributor.authorSormunen, Raija
dc.contributor.authorNasheuer, Heinz-Peter
dc.contributor.authorNethanel, Tamar
dc.contributor.authorKaufmann, Gabriel
dc.contributor.authorPospiech, Helmut
dc.contributor.authorSyväoja, Juhani E.
dc.date.accessioned2018-08-24T08:26:19Z
dc.date.available2018-08-24T08:26:19Z
dc.date.issued2006-11-15
dc.identifier.citationRytkönen, Anna K. Hillukkala, Tomi; Vaara, Markku; Sokka, Miiko; Jokela, Maarit; Sormunen, Raija; Nasheuer, Heinz-Peter; Nethanel, Tamar; Kaufmann, Gabriel; Pospiech, Helmut; Syväoja, Juhani E. (2006). Dna polymerase ε associates with the elongating form of rna polymerase ii and nascent transcripts. FEBS Journal 273 (24), 5535-5549
dc.identifier.issn1742-464X,1742-4658
dc.identifier.urihttp://hdl.handle.net/10379/9836
dc.description.abstractDNA polymerase epsilon co-operates with polymerases alpha and delta in the replicative DNA synthesis of eukaryotic cells. We describe here a specific physical interaction between DNA polymerase epsilon and RNA polymerase II, evidenced by reciprocal immunoprecipitation experiments. The interacting RNA polymerase II was the hyperphosphorylated IIO form implicated in transcriptional elongation, as inferred from (a) its reduced electrophoretic mobility that was lost upon phosphatase treatment, (b) correlation of the interaction with phosphorylation of Ser5 of the C-terminal domain heptapeptide repeat, and (c) the ability of C-terminal domain kinase inhibitors to abolish it. Polymerase epsilon was also shown to UV crosslink specifically alpha-amanitin-sensitive transcripts, unlike DNA polymerase alpha that crosslinked only to RNA-primed nascent DNA. Immunofluorescence microscopy revealed partial colocalization of RNA polymerase IIO and DNA polymerase epsilon, and immunoelectron microscopy revealed RNA polymerase IIO and DNA polymerase epsilon in defined nuclear clusters at various cell cycle stages. The RNA polymerase IIO-DNA polymerase epsilon complex did not relocalize to specific sites of DNA damage after focal UV damage. Their interaction was also independent of active DNA synthesis or defined cell cycle stage.
dc.publisherWiley-Blackwell
dc.relation.ispartofFEBS Journal
dc.subjectDNA polymerase epsilon
dc.subjectDNA replication
dc.subjectimmunoelectron microscopy
dc.subjectnucleotide excision repair
dc.subjectrna polymerase ii
dc.subjectnucleotide excision-repair
dc.subjectcarboxyl-terminal domain
dc.subjectcell nuclear antigen
dc.subjectsaccharomyces-cerevisiae
dc.subjectin-vitro
dc.subjects-phase
dc.subjectreplication
dc.subjectholoenzyme
dc.subjectprotein
dc.subjectalpha
dc.titleDna polymerase ε associates with the elongating form of rna polymerase ii and nascent transcripts
dc.typeArticle
dc.identifier.doi10.1111/j.1742-4658.2006.05544.x
dc.local.publishedsourcehttp://onlinelibrary.wiley.com/doi/10.1111/j.1742-4658.2006.05544.x/pdf
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