- EMDB-50228: Human DNA Polymerase epsilon bound to T-C mismatched DNA (Mismatc... -
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基本情報
登録情報
データベース: EMDB / ID: EMD-50228
タイトル
Human DNA Polymerase epsilon bound to T-C mismatched DNA (Mismatch Excision state)
マップデータ
試料
複合体: Quaternary Complex of human leading strand polymerase epsilon, Proliferating cell nuclear antigen (PCNA), substrate DNA and incoming nucleotide.
複合体: DNA polymerase epsilon catalytic subunit A
タンパク質・ペプチド: DNA polymerase epsilon catalytic subunit A
複合体: DNA
DNA: DNA nascent strand
DNA: DNA template strand
リガンド: IRON/SULFUR CLUSTER
リガンド: CALCIUM ION
キーワード
DNA / polymerase / epsilon / PCNA / leading strand / human / replication / replisome / proofreading
機能・相同性
機能・相同性情報
DNA replication initiation / epsilon DNA polymerase complex / single-stranded DNA 3'-5' DNA exonuclease activity / Activation of the pre-replicative complex / 加水分解酵素; エステル加水分解酵素; 5'-リン酸モノエステル産生エンドデオキシリボヌクレアーゼ / nucleotide-excision repair, DNA gap filling / DNA replication proofreading / DNA synthesis involved in DNA repair / leading strand elongation / PCNA-Dependent Long Patch Base Excision Repair ...DNA replication initiation / epsilon DNA polymerase complex / single-stranded DNA 3'-5' DNA exonuclease activity / Activation of the pre-replicative complex / 加水分解酵素; エステル加水分解酵素; 5'-リン酸モノエステル産生エンドデオキシリボヌクレアーゼ / nucleotide-excision repair, DNA gap filling / DNA replication proofreading / DNA synthesis involved in DNA repair / leading strand elongation / PCNA-Dependent Long Patch Base Excision Repair / embryonic organ development / base-excision repair, gap-filling / Gap-filling DNA repair synthesis and ligation in GG-NER / Recognition of DNA damage by PCNA-containing replication complex / Termination of translesion DNA synthesis / HDR through Homologous Recombination (HRR) / G1/S transition of mitotic cell cycle / Dual Incision in GG-NER / DNA-templated DNA replication / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / mitotic cell cycle / 4 iron, 4 sulfur cluster binding / DNA replication / DNA-directed DNA polymerase / DNA-directed DNA polymerase activity / chromatin binding / nucleotide binding / DNA binding / zinc ion binding / nucleoplasm / nucleus / plasma membrane 類似検索 - 分子機能
DNA polymerase epsilon, catalytic subunit A, C-terminal / DNA polymerase epsilon catalytic subunit / Domain of unknown function (DUF1744) / DUF1744 / DNA polymerase family B, thumb domain / DNA polymerase family B / DNA polymerase family B, exonuclease domain / DNA-directed DNA polymerase, family B, exonuclease domain / DNA-directed DNA polymerase, family B, multifunctional domain / DNA polymerase, palm domain superfamily ...DNA polymerase epsilon, catalytic subunit A, C-terminal / DNA polymerase epsilon catalytic subunit / Domain of unknown function (DUF1744) / DUF1744 / DNA polymerase family B, thumb domain / DNA polymerase family B / DNA polymerase family B, exonuclease domain / DNA-directed DNA polymerase, family B, exonuclease domain / DNA-directed DNA polymerase, family B, multifunctional domain / DNA polymerase, palm domain superfamily / DNA polymerase type-B family / DNA-directed DNA polymerase, family B / Ribonuclease H superfamily / Ribonuclease H-like superfamily / DNA/RNA polymerase superfamily 類似検索 - ドメイン・相同性
DNA polymerase epsilon catalytic subunit A 類似検索 - 構成要素
ジャーナル: Nat Struct Mol Biol / 年: 2024 タイトル: Structural basis for processive daughter-strand synthesis and proofreading by the human leading-strand DNA polymerase Pol ε. 著者: Johann J Roske / Joseph T P Yeeles / 要旨: During chromosome replication, the nascent leading strand is synthesized by DNA polymerase epsilon (Pol ε), which associates with the sliding clamp processivity factor proliferating cell nuclear ...During chromosome replication, the nascent leading strand is synthesized by DNA polymerase epsilon (Pol ε), which associates with the sliding clamp processivity factor proliferating cell nuclear antigen (PCNA) to form a processive holoenzyme. For high-fidelity DNA synthesis, Pol ε relies on nucleotide selectivity and its proofreading ability to detect and excise a misincorporated nucleotide. Here, we present cryo-electron microscopy (cryo-EM) structures of human Pol ε in complex with PCNA, DNA and an incoming nucleotide, revealing how Pol ε associates with PCNA through its PCNA-interacting peptide box and additional unique features of its catalytic domain. Furthermore, by solving a series of cryo-EM structures of Pol ε at a mismatch-containing DNA, we elucidate how Pol ε senses and edits a misincorporated nucleotide. Our structures delineate steps along an intramolecular switching mechanism between polymerase and exonuclease activities, providing the basis for a proofreading mechanism in B-family replicative polymerases.