2KHU

Solution Structure of the Ubiquitin-Binding Motif of Human Polymerase Iota

2KHU の概要

• エントリーDOI: 10.2210/pdb2khu/pdb
• 関連するPDBエントリー: 2KHW
• NMR情報: BMRB: 16882
• 分子名称: Immunoglobulin G-binding protein G, DNA polymerase iota (1 entity in total)
• 機能のキーワード: ubm, ubiquitin-binding domain, polymerase iota, translesion synthesis, tls, immunoglobulin g-binding protein, ubiquitin-binding protein, transferase-protein binding complex, transferase/protein binding
• 由来する生物種: Streptococcus sp., Homo sapiens
• 細胞内の位置: Nucleus: Q9UNA4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12348.56

構造登録者

Bomar, M.G.,D'Souza, S.,Bienko, M.,Dikic, I.,Walker, G. (登録日: 2009-04-11, 公開日: 2010-02-23, 最終更新日: 2024-05-22)

主引用文献

Bomar, M.G.,D'Souza, S.,Bienko, M.,Dikic, I.,Walker, G.C.,Zhou, P.
Unconventional Ubiquitin Recognition by the Ubiquitin-Binding Motif within the Y Family DNA Polymerases iota and Rev1.
Mol.Cell, 37:408-417, 2010

PubMed Abstract: Translesion synthesis is an essential cell survival strategy to promote replication after DNA damage. The accumulation of Y family polymerases (pol) iota and Rev1 at the stalled replication machinery is mediated by the ubiquitin-binding motifs (UBMs) of the polymerases and enhanced by PCNA monoubiquitination. We report the solution structures of the C-terminal UBM of human pol iota and its complex with ubiquitin. Distinct from other ubiquitin-binding domains, the UBM binds to the hydrophobic surface of ubiquitin centered at L8. Accordingly, mutation of L8A, but not I44A, of ubiquitin abolishes UBM binding. Human pol iota contains two functional UBMs, both contributing to replication foci formation. In contrast, only the second UBM of Saccharomyces cerevisiae Rev1 binds to ubiquitin and is essential for Rev1-dependent cell survival and mutagenesis. Point mutations disrupting the UBM-ubiquitin interaction also impair the accumulation of pol iota in replication foci and Rev1-mediated DNA damage tolerance in vivo.

PubMed: 20159559
DOI: 10.1016/j.molcel.2009.12.038

実験手法

SOLUTION NMR