- EMDB-2789: Cryo-EM map of the Timeless-Tipin-RPA Complex -
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基本情報
登録情報
データベース: EMDB / ID: EMD-2789
タイトル
Cryo-EM map of the Timeless-Tipin-RPA Complex
マップデータ
Reconstruction of the Timless-Tipin-RPA complex
試料
試料: Timeless-Tipin-RPA complex
タンパク質・ペプチド: Timeless
タンパク質・ペプチド: Timeless-interacting protein
タンパク質・ペプチド: Replication protein A 70
タンパク質・ペプチド: Replication protein A 32
タンパク質・ペプチド: Replication protein A 14
キーワード
Timeless / Tipin / Replication protein A / RPA / DNA replication
機能・相同性
機能・相同性情報
Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) / : / Activation of ATR in response to replication stress / Removal of the Flap Intermediate / PCNA-Dependent Long Patch Base Excision Repair / Removal of the Flap Intermediate from the C-strand / Activation of the pre-replicative complex / Presynaptic phase of homologous DNA pairing and strand exchange / Regulation of HSF1-mediated heat shock response ...Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta) / : / Activation of ATR in response to replication stress / Removal of the Flap Intermediate / PCNA-Dependent Long Patch Base Excision Repair / Removal of the Flap Intermediate from the C-strand / Activation of the pre-replicative complex / Presynaptic phase of homologous DNA pairing and strand exchange / Regulation of HSF1-mediated heat shock response / SUMOylation of DNA damage response and repair proteins / Gap-filling DNA repair synthesis and ligation in GG-NER / Fanconi Anemia Pathway / HDR through Single Strand Annealing (SSA) / Translesion synthesis by REV1 / Translesion synthesis by POLK / cellular response to bleomycin / Translesion synthesis by POLI / Recognition of DNA damage by PCNA-containing replication complex / HDR through Homologous Recombination (HRR) / G2/M DNA damage checkpoint / Translesion Synthesis by POLH / Termination of translesion DNA synthesis / Dual Incision in GG-NER / Dual incision in TC-NER / Formation of Incision Complex in GG-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / protein localization to chromosome / : / replication fork arrest / Processing of DNA double-strand break ends / DNA replication factor A complex / cell cycle phase transition / cellular response to cisplatin / cellular response to hydroxyurea / Regulation of TP53 Activity through Phosphorylation / lateral element / single-stranded telomeric DNA binding / DNA replication checkpoint signaling / regulation of DNA damage checkpoint / positive regulation of circadian rhythm / replication fork protection complex / G-rich strand telomeric DNA binding / mitotic intra-S DNA damage checkpoint signaling / positive regulation of double-strand break repair / branching involved in ureteric bud morphogenesis / regulation of double-strand break repair via homologous recombination / branching morphogenesis of an epithelial tube / DNA unwinding involved in DNA replication / site of DNA damage / hemopoiesis / telomere maintenance via telomerase / positive regulation of double-strand break repair via homologous recombination / chromosome organization / mismatch repair / mitotic G1 DNA damage checkpoint signaling / response to UV / condensed chromosome / homeostasis of number of cells within a tissue / regulation of mitotic cell cycle / telomere maintenance / kidney development / DNA damage checkpoint signaling / condensed nuclear chromosome / male germ cell nucleus / meiotic cell cycle / morphogenesis of an epithelium / nucleotide-excision repair / lung development / double-strand break repair via homologous recombination / regulation of circadian rhythm / base-excision repair / PML body / circadian rhythm / single-stranded DNA binding / site of double-strand break / regulation of cell population proliferation / protein phosphatase binding / in utero embryonic development / DNA replication / damaged DNA binding / chromosome, telomeric region / nuclear body / cell division / DNA repair / negative regulation of DNA-templated transcription / DNA damage response / ubiquitin protein ligase binding / positive regulation of cell population proliferation / chromatin binding / chromatin / negative regulation of transcription by RNA polymerase II / enzyme binding / DNA binding / nucleoplasm / nucleus / metal ion binding / cytoplasm 類似検索 - 分子機能
Replication factor A protein 2 / Replication factor A protein 2 / Replication protein A, C-terminal / Replication protein A C terminal / Replication factor A protein 3 / Replication factor A protein 3 / Replication factor A protein 3 / Timeless, C-terminal / Timeless PAB domain / Replication factor A protein-like ...Replication factor A protein 2 / Replication factor A protein 2 / Replication protein A, C-terminal / Replication protein A C terminal / Replication factor A protein 3 / Replication factor A protein 3 / Replication factor A protein 3 / Timeless, C-terminal / Timeless PAB domain / Replication factor A protein-like / Replication factor-A protein 1, N-terminal domain / Chromosome segregation in meiosis protein 3 / Chromosome segregation in meiosis protein 3 / TIPIN/Csm3/Swi3 / Replication Fork Protection Component Swi3 / Replication factor A protein 1 / Replication factor A protein 1 / Replication factor-A protein 1, N-terminal / Replication protein A, OB domain / Replication protein A OB domain / Timeless, N-terminal / Timeless, N-terminal / Timeless protein / Replication factor A, C-terminal / Replication factor-A C terminal domain / OB-fold nucleic acid binding domain, AA-tRNA synthetase-type / OB-fold nucleic acid binding domain / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily / Nucleic acid-binding, OB-fold 類似検索 - ドメイン・相同性
Replication protein A 32 kDa subunit / Replication protein A 70 kDa DNA-binding subunit / TIMELESS-interacting protein / Replication protein A 14 kDa subunit / Protein timeless homolog 類似検索 - 構成要素
ジャーナル: Nucleic Acids Res / 年: 2014 タイトル: Architecture and ssDNA interaction of the Timeless-Tipin-RPA complex. 著者: Justine Witosch / Eva Wolf / Naoko Mizuno / 要旨: The Timeless-Tipin (Tim-Tipin) complex, also referred to as the fork protection complex, is involved in coordination of DNA replication. Tim-Tipin is suggested to be recruited to replication forks ...The Timeless-Tipin (Tim-Tipin) complex, also referred to as the fork protection complex, is involved in coordination of DNA replication. Tim-Tipin is suggested to be recruited to replication forks via Replication Protein A (RPA) but details of the interaction are unknown. Here, using cryo-EM and biochemical methods, we characterized complex formation of Tim-Tipin, RPA and single-stranded DNA (ssDNA). Tim-Tipin and RPA form a 258 kDa complex with a 1:1:1 stoichiometry. The cryo-EM 3D reconstruction revealed a globular architecture of the Tim-Tipin-RPA complex with a ring-like and a U-shaped domain covered by a RPA lid. Interestingly, RPA in the complex adopts a horse shoe-like shape resembling its conformation in the presence of long ssDNA (>30 nucleotides). Furthermore, the recruitment of the Tim-Tipin-RPA complex to ssDNA is modulated by the RPA conformation and requires RPA to be in the more compact 30 nt ssDNA binding mode. The dynamic formation and disruption of the Tim-Tipin-RPA-ssDNA complex implicates the RPA-based recruitment of Tim-Tipin to the replication fork.