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Error-free insertion in cyclobutane pyrimidine bypass is due mainly to pol eta (translesion synthesis TLS3) in oocyte extracts during DNA replication.
A substantial excess of single and tandem somatic mutations within known pol eta mutable motifs was noted in skin cancer as well as in many other types of human cancer.
In addition to the two Mg(2+) ions aligning the active site of DNA polymerase eta, experiments suggest that a third Mg(2+) ion could play an essential catalytic role. The simulations with three metal ions in the active site suggest that the third metal ion may play a catalytic role through electrostatic interactions with the leaving group.
Findings demonstrate a novel role of Poleta O-GlcNAcylation in translesion DNA synthesis regulation and genome stability maintenance.
Rad18, independently of its ubiquitin ligase activity, promotes DNA polymerase eta SUMOylation by facilitating its interaction with its SUMO ligase PIAS1 and is required for DNA polymerase eta function at difficult to replicate loci.
In human DNA polymerase eta, the conserved Arg61 favors Watson-Crick base pairing through defined interactions with the incoming nucleotide.
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.
Two novel mutations in the POLH gene, which encodes the translesion DNA polymerase eta, with loss of function due to two independent exon skippings, are reported to be associated as a compound heterozygous state in the patient.
Data suggest that DNA polymerase eta (POLH/RAD30) is able to bind DNA/DNA, RNA/DNA, and DNA/RNA duplexes with similar affinities; DNA polymerase eta (as well as DNA polymerase kappa) accommodates RNA as one of the two strands during primer extension; both polymerases elongate RNA/DNA and DNA/RNA hybrids; additionally, DNA polymerase eta catalyzes reverse transcription.
Poleta fulfills an important role in managing replicative stress at alternative lengthening of telomeres.
POLH is phosphorylated by CDK2.POLH serine 687 is a CDK target and is regulated during the cell cycle.POLH phosphorylation controls protein stability.
The current work explores both the fidelity of DNA polymerase eta and the role of the 3rd metal ion (magnesium), by using empirical valence bond simulations.
The results suggest that translesion synthesis by Pol eta can contribute to the accumulation of rCMP in the genome, particularly opposite modified guanines.
the targeting of Poleta to damage sites after UV exposure is regulated by SPARTAN, and this function contributes highly to its DNA-damage tolerance function.
Study shows that the posttranslational modifications of nuclear localization signal of pol eta played a dual role in polymerase switching, where Lys682 deubiquitination promotes the recruitment of pol eta to PCNA immediately prior to lesion bypass and Ser687 phosphorylation stimulates its departure from the replication fork immediately after lesion bypass.
The data directly show that, in the human genome, DNA Pol-eta and Rev1 bypass cyclobutane pyrimidine dimers and 6-4PP at replication forks, while only 6-4PP are also tolerated by a Rev3L-dependent gap-filling mechanism, independent of S phase.
p53 controls the induction of DNA polymerase eta in DNA damaged human cells. The role of DNA polymerase eta in p53-dependent translesion synthesis.
DNA polymerases eta and kappa are capable of bypassing of a bulky guanine lesion during DNA replication.
These results provide important knowledge about the effects of the length and structure of the alkyl group in O(4)-alkylthymidine lesions on the fidelity and efficiency of DNA replication mediated by human DNA polymerase eta.
The described is cooperative motion of a key positively charged residue and metal ions for DNA replication catalyzed by human DNA Polymerase eta.
free energy difference is slightly greater for binding at the 5' thymine position than at the 3' thymine position, presumably because of stabilization arising from the A:T base pair formed at the 3' position of the TTD in previous step of Pol eta function
the functions of REV3L in maintaining cell viability, embryonic viability and genomic stability are directly dependent on its polymerase activity, and cannot be ameliorated by an additional deletion of pol eta.
XP-V has a role in adipose tissue senescence and metabolic syndrome
Increase in UV-induced mutations at both G:C and A:T pairs associated with PolH deficiency suggests that PolH contributes to accurate translesion synthesis (TLS) past both T- & C-containing dimers.
POLH deficiency did not affect the frequency and patterns of C:G mutations and UNG POLH double deficiency showed an additive effect of single deficiency.
REV1 and Polkappa are involved in DNA damage tolerance via Poleta-REV1 interaction when Poleta fails to bypass its cognate substrates.
These results reveal genetic interactions between REV1 catalytic activity and POLH and identify an alternative pathway in the generation of C to G and G to C transversions.
these data support the existence of PCNA ubiquitination-dependent and -independent activation pathways of Poleta during somatic hypermutation and DNA damage tolerance.
inaccurate DNA synthesis by mammalian DNA polymerase eta (pol eta) contributes to somatic hypermutation (SHM) of Ig genes
suggest the involvement of the Pol eta and Pol iota proteins in UV-induced skin carcinogenesis
Results reveal genetic and biochemical interactions between DNA polymerases eta (POLH) and theta (POLQ) and suggest that POLQ might cooperate with POLH to generate some of the A/T mutations during the somatic hypermutation of Ig genes.
results demonstrate that POLH is a limiting factor for A:T mutations and contributes to the efficient diversification of Ig genes and affinity maturation of antibodies
observe upon the simultaneous knockdown of Pols kappa and zeta implicates a highly error-free role of Poleta in TLS opposite cyclobutane pyrimidine dimers in mammalian cells.
DNA polymerase fidelity and specificity
This gene encodes a member of the Y family of specialized DNA polymerases. It copies undamaged DNA with a lower fidelity than other DNA-directed polymerases. However, it accurately replicates UV-damaged DNA\; when thymine dimers are present, this polymerase inserts the complementary nucleotides in the newly synthesized DNA, thereby bypassing the lesion and suppressing the mutagenic effect of UV-induced DNA damage. This polymerase is thought to be involved in hypermutation during immunoglobulin class switch recombination. Mutations in this gene result in XPV, a variant type of xeroderma pigmentosum.
DNA-directed DNA polymerase eta
, DNA polymerase eta
, polymerase (DNA directed), eta
, DNA polymerase eta-like
, polymerase eta
, RAD30 homolog A
, xeroderma pigmentosum variant type protein
, polymerase (DNA directed), eta (RAD 30 related)
, xeroderma pigmentosum variant type protein homolog