tailieunhanh - Báo cáo khoa học: DNA polymerase e associates with the elongating form of RNA polymerase II and nascent transcripts

DNA polymeraseeco-operates with polymerasesaanddin the replicative DNA synthesis of eukaryotic cells. We describe here a specific physical interaction between DNA polymerase eand RNA polymerase II, evidenced by reciprocal immunoprecipitation experiments. The interacting RNA polymerase II was the hyperphosphorylated IIO form implicated in tran- | ỊFEBS Journal DNA polymerase e associates with the elongating form of RNA polymerase II and nascent transcripts Anna K. Rytkonen1 2 Tomi Hillukkala1 Markku Vaara2 Miiko Sokka2 Maarit Jokela1 4 Raija Sormunen3 Heinz-Peter Nasheuer4 Tamar Nethanel5 Gabriel Kaufmann5 Helmut Pospiech1 and Juhani E. Syvaoja2 1 Biocenter Oulu and Department of Biochemistry University of Oulu Finland 2 Department of Biology University of Joensuu Finland 3 Biocenter Oulu and Department of Pathology University of Oulu Finland 4 NationalUniversity of Ireland Department of Biochemistry CellCycle ControlLaboratory Galway Ireland 5 Department of Biochemistry TelAviv University Ramat Aviv Israel Keywords DNA polymerase e DNA replication immunoelectron microscopy nucleotide excision repair RNA polymerase II Correspondence H. Pospiech Department of Biochemistry PO Box 3000 FIN-90014 Oulu Finland Fax 358 8 5531141 Tel 358 8 5531155 E-mail tPresent address Department of InternalMedicine University of Oulu Finland These authors contributed equally to this work Received 15 September 2006 revised 16 October 2006 accepted 18 October 2006 doi DNA polymerase e co-operates with polymerases a and Ỗ in the replicative DNA synthesis of eukaryotic cells. We describe here a specific physical interaction between DNA polymerase e 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 e was also shown to UV crosslink specifically a-amanitin-sensitive transcripts unlike DNA polymerase a that crosslinked only to RNA-primed nascent DNA. .

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