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This study found that human DNA Polymerase kappa is more tolerant to changes in the active site loop than E. coli DinB. [DinB]
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Two X-ray crystal structures of POLK provide mechanistic insights into the error-free lucidin-N(2)-dG DNA adduct bypass catalyzed by POLK.
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POLH & POLK are both able to exchange with PolD1 stalled at repetitive CFS (common fragile sites) sequences. POLD1 synthesis was inhibited by replication stress caused by aphidicolin, preventing any replication past CFS. Importantly, POLH & POLK were still proficient in rescuing this stalled POLD1 synthesis. POLD1 stalling at CFSs allows for free exchange with specialized polymerase that is not driven by PCNA.
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Data suggest that error-free DNA replication through 3-deaza-3-methyladenine adduct is mediated via three different pathways dependent upon POL-iota/POL-kappa, POL-theta, and POL-zeta.
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The structure of polK captured at the lesion-extension stage is reported: the enzyme is extending the primer strand after the base pair containing the BP-dG adduct in the template strand at the -1 position. PolK accommodates the BP adduct in the nascent DNA's minor groove and keeps the adducted DNA helix in a B-form.
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A report on the structure of human polkappa in complex with a major benzo[a]pyrene adduct reveal a unique mechanism for accurate replication by translesion synthesis past the major bulky adduct.
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These studies revealed that POLK is a crucial host factor required for covalently closed circular DNA formation during a de novo HBV infection
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DNA polymerases eta and kappa are capable of bypassing of a bulky guanine lesion during DNA replication.
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POLK protein polymorphisms may influence the risk of developing breast cancer among Chinese women.
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Somatic Mutations in Catalytic Core of POLK Reported in Prostate Cancer Alter Translesion DNA Synthesis
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POLK not only protects cells from genotoxic DNA lesions via DNA polymerase activities, but also contributes to genome integrity by acting as a non-catalytic protein against oxidative damage caused by hydrogen peroxide and menadione.
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The steric gate is crucial for rNTP discrimination because of its role in specifically promoting a dNTP-induced conformational change and that rNTP discrimination occurs in a relatively closed state of the polymerases.
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The structural dynamics of DinB1 changes upon substrate binding, noncognate DNA damage prevents the formation of the active conformation of DINB1.
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polymorphism of POLK, an important gene in TLS, participates in platinum-chemotherapy tolerance and side-effect
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The study shows that the Werner syndrome protein stimulates the 8-oxo-dG bypass activity of hpol kappa in vitro by enhancing the correct base insertion opposite the lesion, as well as extension from dC:8-oxo-dG base pairs.
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Mutations in PIP1 domain inhibits the stimulation of DNA synthesis by Polkappa in the presence of proliferating cell nuclear antigen, replication factor C, and replication protein A; and mutations in PIP2 have no effect on PCNA-dependent DNA synthesis.
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The truncation R219X was devoid of polymerase activity, and the E419G and Y432S variants showed much lower polymerase activity than wild-type POLK.
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A slow conformational change after the nucleotidyl transfer is the rate-limiting step for hpol kappa catalysis.
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role of the unique Polkappa gap and N-clasp structural features in the fidelity of minor groove lesion processing with extensive molecular modeling and molecular dynamics simulations to pinpoint their functioning in lesion bypass
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Phenylalanine 171 is used by PolK as a molecular brake for translesional synthesis across benzo[a]pyrene DNA adducts.
