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Human Polyclonal POLK Primary Antibody pour ELISA, WB - ABIN539465
Haracska, Prakash, Prakash: A mechanism for the exclusion of low-fidelity human Y-family DNA polymerases from base excision repair. dans Genes & development 2003
Show all 3 Pubmed References
Human Monoclonal POLK Primary Antibody pour IF, IHC (p) - ABIN565606
Sekimoto, Oda, Kurashima, Hanaoka, Yamashita: Both high-fidelity replicative and low-fidelity Y-family polymerases are involved in DNA rereplication. dans Molecular and cellular biology 2015
Human Polyclonal POLK Primary Antibody pour IF, WB - ABIN6685484
Xiang, Laurent, Hsu, Nachtergaele, Lu, Sheng, Xu, Chen, Ouyang, Wang, Ling, Hsu, Zou, Jambhekar, He, Shi: RNA m6A methylation regulates the ultraviolet-induced DNA damage response. dans Nature 2017
observations from molecular dynamics simulations suggest a possible explanation for the observed experimental results that pol kappa adopts specific active and inactive conformations that depend on both the protein variant and the identity of the DNA adduct
Biochemical and structural work provides the basis for the mechanism by which polkappa performs the error-free and efficient replication across the major cisplatin lesion at the second insertion and extension stages. Polkappa accommodates the highly flexible Pt-GG adduct in a stable conformation, which minimizes the instability of the replicating base pair.
These results suggest that POLK genetic polymorphism rs73120833 plays an important role on the prognosis of small cell lung cancer patients, which can be potential genetic biomarker for small cell lung cancer personalized treatment.
This study found that human DNA Polymerase kappa is more tolerant to changes in the active site loop than E. coli DinB. [DinB]
Two X-ray crystal structures of POLK provide mechanistic insights into the error-free lucidin-N(2)-dG DNA adduct bypass catalyzed by POLK.
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.
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 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.
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.
These studies revealed that POLK is a crucial host factor required for covalently closed circular DNA formation during a de novo HBV infection
DNA polymerases eta and kappa are capable of bypassing of a bulky guanine lesion during DNA replication.
POLK protein polymorphisms may influence the risk of developing breast cancer among Chinese women.
Somatic Mutations in Catalytic Core of POLK Reported in Prostate Cancer Alter Translesion DNA Synthesis
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.
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.
The structural dynamics of DinB1 changes upon substrate binding, noncognate DNA damage prevents the formation of the active conformation of DINB1.
polymorphism of POLK, an important gene in TLS, participates in platinum-chemotherapy tolerance and side-effect
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.
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.
The truncation R219X was devoid of polymerase activity, and the E419G and Y432S variants showed much lower polymerase activity than wild-type POLK.
The results indicate that Polkappa does not suppress benzo[a]pyrene -induced mutagenesis and carcinogenesis in the colon, but counteracts inflammation-induced mutagenesis in multiple organs.
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 is required for the processivity and fidelity of Polkappa 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 is essential for the structural integrity and flexibility of Polkappa during translesion synthesis.
Polkappa 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
Data suggest that DNA polymerase kappa Polkappa functions in DNA interstrand crosslinks (ICLs) repair in embryonic fibroblast cells (MEF), especially during the G0/G1 phases.
solution structure of the polymerase kappa-Rev1 complex
in mammalian cells, both polymerases kappa and iota are necessary for the error-free bypass of N(2)-CEdG and N(2)-CMdG.
results are consistent with the notion that Pol kappa is required for accurate translesion DNA synthesis past naturally occurring polycyclic guanine adducts, possibly generated by cholesterol and/or its metabolites.
Polkappa plays an important role in suppressing mutations at DNA lesions generated by benzo[a]pyrene, but not UV or x-ray irradiation.
Rev7 competes directly with Pol kappa for binding to the Rev1 C-terminus.
The multiple mouse/human (PolK/POLK) transcripts may encode multiple Polkappa isoforms in testis
the trans-lesion synthesis enzyme polkappa is specifically required for normal recovery from the BPDE-induced S-phase checkpoint
Pol kappa and Pol iota double-deficient mice had the normal somatic hypermutation frequency
Polk causes error-prone and inefficient replication across 8-oxoguanine in ras genes.
Polkappa has a function in translesion DNA synthesis past alkylated base adducts as well as UV radiation DNA damage in vertebrates
compromised translesion synthesis in Polkappa(-/-) mice may result in replication fork pausing which, in turn, may affect expanded simple tandem repeat mutation rate
pol kappa-deficient mouse cells have substantially reduced (but not absent) levels of nucleotide excision repair
DNA polymerase kappa-dependent DNA synthesis at stalled replication forks is important for CHK1 activation.
Data show that DNA polymerase kappa (Pol kappa) is essential for replication-independent ICL repair (RIR) of a site-specific DNA interstrand crosslinks (ICLs) lesion.
pol kappa (translesion synthesis TLS4) may assist pol eta (TLS3 or Rad30) in error-free extension during cyclobutane pyrimidine dimer bypass during DNA replication in oocyte extracts.
SUMO-mediated regulation of both POLH-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