Point mutations in Escherichia coli DNA pol V that confer resistance to non-cognate DNA damage also alter protein–protein interactions

Hawver, Lisa A.; Tehrani, Mohammad Mehdi; Antczak, Nicole M.; Kania, Danielle; Muser, Stephanie; Sefcikova, Jana; Beuning, Penny J.

doi:10.1016/j.mrfmmm.2015.07.003

Cited by 6 publications

(1 citation statement)

References 89 publications

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“…Decades of intense research have revealed the complex levels of Pol V regulation in increasing detail. However, the lack of experimental 3D structures of Pol V or even its catalytic subunit, UmuC, preclude the comprehensive understanding of the interactions relevant to the assembly and mechanism of Pol V. UmuC and DinB share a conserved Y-family core, therefore, the core structure of UmuC could be derived by homology modeling (11,12). However, unlike DinB, UmuC has an additional C-terminal extension that has no obvious relationship with known structures.…”

Section: Introductionmentioning

confidence: 99%

New insights into the structures and interactions of bacterial Y-family DNA polymerases

Timinskas

Venclovas

2019

Nucleic Acids Research

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Bacterial Y-family DNA polymerases are usually classified into DinB (Pol IV), UmuC (the catalytic subunit of Pol V) and ImuB, a catalytically dead essential component of the ImuA-ImuB-DnaE2 mutasome. However, the true diversity of Y-family polymerases is unknown. Furthermore, for most of them the structures are unavailable and interactions are poorly characterized. To gain a better understanding of bacterial Y-family DNA polymerases, we performed a detailed computational study. It revealed substantial diversity, far exceeding traditional classification. We found that a large number of subfamilies feature a C-terminal extension next to the common Y-family region. Unexpectedly, in most C-terminal extensions we identified a region homologous to the N-terminal oligomerization motif of RecA. This finding implies a universal mode of interaction between Y-family members and RecA (or ImuA), in the case of Pol V strongly supported by experimental data. In gram-positive bacteria, we identified a putative Pol V counterpart composed of a Y-family polymerase, a YolD homolog and RecA. We also found ImuA-ImuB-DnaE2 variants lacking ImuA, but retaining active or inactive Y-family polymerase, a standalone ImuB C-terminal domain and/or DnaE2. In summary, our analyses revealed that, despite considerable diversity, bacterial Y-family polymerases share previously unanticipated similarities in their structural domains/motifs and interactions.

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Section: Introductionmentioning

confidence: 99%

New insights into the structures and interactions of bacterial Y-family DNA polymerases

Timinskas

Venclovas

2019

Nucleic Acids Research

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Site‐Specific N²‐dG DNA Adducts: Formation, Synthesis, and TLS Polymerase‐Mediated Bypass

Ghodke

Pradeepkumar

2020

Eur J Org Chem

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The N2‐position of deoxyguanosine (dG) in DNA is susceptible to modification by various damaging agents. These modifications (lesions or adducts) can stall the DNA replication by replicative polymerases, and if the common DNA repair pathways do not remove them, it can result in genomic instability. This generally leads to the death or oncogenic transformation of the cell. An important mechanism to deal with this problem is Translesion synthesis (TLS), a bypass mechanism, which involves the tolerance of DNA damage by low‐fidelity DNA polymerases (TLS polymerases). To understand the accuracy of TLS polymerases, a chemical biology approach is required. In this review, we discuss the reliable methods to synthesize specific N2‐dG DNA adducts and how they are tolerated by bacterial TLS polymerase Pol IV and its mammalian orthologue hpol κ. Molecular insights on the accurate bypass of these adducts emerge from the primer extension assays, X‐ray crystallographic, and molecular modeling studies are reviewed here.

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DNA repair | UmuDC Lesion Bypass DNA Polymerase V

Beuning¹,

Stern²,

Dilworth³

2021

Encyclopedia of Biological Chemistry III

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Point mutations in Escherichia coli DNA pol V that confer resistance to non-cognate DNA damage also alter protein–protein interactions

Cited by 6 publications

References 89 publications

New insights into the structures and interactions of bacterial Y-family DNA polymerases

New insights into the structures and interactions of bacterial Y-family DNA polymerases

Site‐Specific N²‐dG DNA Adducts: Formation, Synthesis, and TLS Polymerase‐Mediated Bypass

DNA repair | UmuDC Lesion Bypass DNA Polymerase V

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Point mutations in Escherichia coli DNA pol V that confer resistance to non-cognate DNA damage also alter protein–protein interactions

Cited by 6 publications

References 89 publications

New insights into the structures and interactions of bacterial Y-family DNA polymerases

New insights into the structures and interactions of bacterial Y-family DNA polymerases

Site‐Specific N2‐dG DNA Adducts: Formation, Synthesis, and TLS Polymerase‐Mediated Bypass

DNA repair | UmuDC Lesion Bypass DNA Polymerase V

Contact Info

Product

Resources

About

Site‐Specific N²‐dG DNA Adducts: Formation, Synthesis, and TLS Polymerase‐Mediated Bypass