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Details on Person Repair of deoxyuridine in DNA is unusually error-prone in pr...
| Class:Id | Summation:9943325 |
|---|---|
| _displayName | Repair of deoxyuridine in DNA is unusually error-prone in pr... |
| _timestamp | 2026-04-26 21:24:08 |
| created | [InstanceEdit:9943318] May, Bruce, 2025-03-27 |
| literatureReference | [LiteratureReference:9943334] Differential expression of APE1 and APE2 in germinal centers promotes error-prone repair and A:T mutations during somatic hypermutation [LiteratureReference:9943357] APE2 Promotes AID-Dependent Somatic Hypermutation in Primary B Cell Cultures That Is Suppressed by APE1 [LiteratureReference:9967625] Base Excision Repair: Mechanisms and Impact in Biology, Disease, and Medicine [LiteratureReference:9967620] A four-subunit DNA polymerase ζ complex containing Pol δ accessory subunits is essential for PCNA-mediated mutagenesis [LiteratureReference:9967644] Complex formation with Rev1 enhances the proficiency of Saccharomyces cerevisiae DNA polymerase zeta for mismatch extension and for extension opposite from DNA lesions [LiteratureReference:9967714] Interaction between the Rev1 C-Terminal Domain and the PolD3 Subunit of Polζ Suggests a Mechanism of Polymerase Exchange upon Rev1/Polζ-Dependent Translesion Synthesis [LiteratureReference:9967711] DNA polymerases ζ and Rev1 mediate error-prone bypass of non-B DNA structures [LiteratureReference:5652047] Ubiquitinated proliferating cell nuclear antigen activates translesion DNA polymerases eta and REV1 |
| modified | [InstanceEdit:9967691] May, Bruce, 2025-10-05 [InstanceEdit:9967728] May, Bruce, 2025-10-06 [InstanceEdit:9975293] May, Bruce, 2025-11-29 [InstanceEdit:9980002] May, Bruce, 2026-01-23 [InstanceEdit:9987697] May, Bruce, 2026-04-26 |
| text | Repair of deoxyuridine in DNA is unusually error-prone in proliferating germinal center B cells. Normally, deoxyuridine is accurately repaired by base excision repair (BER) involving the enzymes Uracil DNA glycosylase (UNG) which excises the uracil base, the endonuclease APEX1 (also called APE1) which converts the abasic site to a nicked single-stranded gap, and the high-fidelity DNA polymerase POLB which synthesizes DNA across the gap (reviewed in Gohil et al. 2023). In germinal center B cells APEX1 expression is reduced and APEX2 expression is increased (inferred from mouse homologs in Stavnezer et al. 2014, Schrader et al. 2023). Unlike APEX1 (APE1), which binds the scaffold protein XRCC1, APEX2 (APE2) directly interacts via its C-terminal region with PCNA (Tsuchimoto et al. 2001, Burkovics et al. 2009). Ubiquitinated PCNA associates with error-prone DNA polymerases POLH (Plosky et al. 2006), POLI (Haracska et al. 2001, 2005, Vidal et al. 2004, Cui et al. 2010), and POLZ (inferred from yeast homologs in Makarova et al. 2012) and the deoxycytidyl transferase REV1 (inferred from yeast homologs in Garg and Burgers 2005) for synthesis across the DNA gap created by APEX2. REV1 also binds POLZ and acts sequentially to insert a cytidine residue followed by translesion synthesis by POLZ (Pustovalova et al. 2016, inferred from yeast homologs in Acharya et al. 2006, Northam et al. 2014). The presence of high APEX2 activity contributes to SHM at variable regions of immunoglobulin genes in cultured B cells (inferred from mouse homologs in Schrader et al. 2023). |
| (summation) | [BlackBoxEvent:9943316] PCNA, APEX2, and error-prone DNA polymerase (POLH, POLI, POLZ, REV1) bind dsDNA with a deoxyribose phosphate residue (abasic site, apurinic/apyrimidinic site, AP site) [Homo sapiens] |
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No pathways have been reviewed or authored by Repair of deoxyuridine in DNA is unusually error-prone in pr... (9943325)
