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Human POLK Protein expressed in Escherichia coli (E. coli) - ABIN2452172
Czerkawski, Blaxter, Wainman: The metabolism of oleic, linoleic and linolenic acids by sheep with reference to their effects on methane production. in The British journal of nutrition 1970
Show all 3 Pubmed References
This study found that human DNA Polymerase kappa (show PAPD7 Proteins) is more tolerant to changes in the active site loop than E. coli DinB. [DinB]
Two X-ray crystal structures of POLK (show PAPD7 Proteins) provide mechanistic insights into the error-free lucidin-N(2)-dG DNA adduct bypass catalyzed by POLK (show PAPD7 Proteins).
POLH (show POLH Proteins) & POLK (show PAPD7 Proteins) are both able to exchange with PolD1 (show POLD1 Proteins) stalled at repetitive CFS (common fragile sites) sequences. POLD1 (show POLD1 Proteins) synthesis was inhibited by replication stress caused by aphidicolin, preventing any replication past CFS. Importantly, POLH (show POLH Proteins) & POLK (show PAPD7 Proteins) were still proficient in rescuing this stalled POLD1 (show POLD1 Proteins) synthesis. POLD1 (show POLD1 Proteins) stalling at CFSs allows for free exchange with specialized polymerase that is not driven by PCNA (show PCNA Proteins).
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.
The structure of polK (show PAPD7 Proteins) 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 (show PAPD7 Proteins) accommodates the BP adduct in the nascent DNA's minor groove and keeps the adducted DNA helix in a B-form.
A report on the structure of human polkappa (show POLL Proteins) in complex with a major benzo[a]pyrene adduct reveal a unique mechanism for accurate replication by translesion synthesis past the major bulky adduct.
These studies revealed that POLK (show PAPD7 Proteins) is a crucial host factor required for covalently closed circular DNA formation during a de novo HBV infection
POLK (show PAPD7 Proteins) protein polymorphisms may influence the risk of developing breast cancer among Chinese women.
Somatic Mutations in Catalytic Core of POLK (show PAPD7 Proteins) Reported in Prostate Cancer Alter Translesion DNA Synthesis
POLK (show PAPD7 Proteins) not only protects cells from genotoxic DNA lesions via DNA polymerase (show POLB Proteins) activities, but also contributes to genome integrity by acting as a non-catalytic protein against oxidative damage caused by hydrogen peroxide and menadione.
The results suggest that Polk has a limited ability to suppress BP-induced genotoxicity in the colon and bone marrow and also that the roles of specialized DNA polymerases in mutagenesis and carcinogenesis should be examined not only by in vitro assays but also by in vivo mouse studies. We also report the spontaneous mutagenesis in inactivated Polk KI mice at young and old ages.
the extreme N-terminal part of Polkappa (show POLL Proteins) is required for the processivity and fidelity of Polkappa (show POLL Proteins) during translesion synthesis of 10S(+)-trans-anti-benzo[a]pyrene diol epoxide-N(2)-deoxyguanine adducts lesions.
Polk plays a predominant role in suppressing point mutations by carrying out error-free translesion DNA synthesis and contributes to the prevention of DNA strand breaks.
The structural gap physically accommodates the bulky aromatic adduct and the N-clasp (show CLASRP Proteins) is essential for the structural integrity and flexibility of Polkappa (show POLL Proteins) during translesion synthesis.
Polkappa (show POLL Proteins) accumulates at laser-induced sites of DNA damage.
Structural basis of Rev1-mediated assembly of a quaternary vertebrate translesion polymerase complex consisting of Rev1, heterodimeric polymerase (Pol) zeta, and Pol kappa (show POLL Proteins)
Data suggest that DNA polymerase kappa Polkapp (show POLL Proteins)a functions in DNA interstrand crosslinks (ICLs) repair in (show APBB1 Proteins) embryonic fibroblast cells (MEF), especially during the G0/G1 phases.
solution structure of the polymerase kappa-Rev1 complex
results are consistent with the notion that Pol kappa (show POLL Proteins) is required for accurate translesion DNA synthesis past naturally occurring polycyclic guanine adducts, possibly generated by cholesterol and/or its metabolites.
Polkappa (show POLL Proteins) plays an important role in suppressing mutations at DNA lesions generated by benzo[a]pyrene, but not UV or x-ray irradiation.
DNA polymerase kappa-dependent DNA synthesis at stalled replication forks is important for CHK1 (show CHEK1 Proteins) activation.
Data show that DNA polymerase kappa (Pol kappa (show POLL Proteins)) is essential for replication-independent ICL repair (RIR (show APBB1 Proteins)) of a site-specific DNA interstrand crosslinks (ICLs) lesion.
pol kappa (show POLL Proteins) (translesion synthesis TLS4) may assist pol eta (TLS3 or Rad30 (show POLH Proteins)) in error-free extension during cyclobutane pyrimidine dimer bypass during DNA replication in oocyte extracts.
SUMO-mediated regulation of both POLH (show POLH Proteins)-1 and POLK-1, and point towards a previously unrecognized role of the nuclear pore in regulating Translesion synthesis .
External and internal DNA-damaging agents continually threaten the integrity of genetic material in cells. Although a variety of repair mechanisms exist to remove the resulting lesions, some lesions escape repair and block the replication machinery. Members of the Y family of DNA polymerases, such as POLK, permit the continuity of the replication fork by allowing replication through such DNA lesions. Each Y family polymerase has a unique DNA-damage bypass and fidelity profile. POLK is specialized for the extension step of lesion bypass (summary by Lone et al., 2007
DNA polymerase kappa
, DNA-directed DNA polymerase kappa
, polymerase (DNA directed) kappa
, DNA polymerase kappa-like
, DINB protein
, DNA damage-inducible protein b
, DinB homolog 1