2KHU
Solution Structure of the Ubiquitin-Binding Motif of Human Polymerase Iota
Summary for 2KHU
Entry DOI | 10.2210/pdb2khu/pdb |
Related | 2KHW |
NMR Information | BMRB: 16882 |
Descriptor | Immunoglobulin G-binding protein G, DNA polymerase iota (1 entity in total) |
Functional Keywords | ubm, ubiquitin-binding domain, polymerase iota, translesion synthesis, tls, immunoglobulin g-binding protein, ubiquitin-binding protein, transferase-protein binding complex, transferase/protein binding |
Biological source | Streptococcus sp., Homo sapiens |
Cellular location | Nucleus: Q9UNA4 |
Total number of polymer chains | 1 |
Total formula weight | 12348.56 |
Authors | Bomar, M.G.,D'Souza, S.,Bienko, M.,Dikic, I.,Walker, G. (deposition date: 2009-04-11, release date: 2010-02-23, Last modification date: 2024-05-22) |
Primary citation | 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 Cited by 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: 20159559DOI: 10.1016/j.molcel.2009.12.038 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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