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DNA polymerase beta is sensitive to Mn2+ and Mg2 (zeige MCOLN1 Proteine)+ and its optimumal pH is 9.
In brief, the major differences in BER performed by early stage embryos and adults are the absence of DNA polymerase-beta, leading to predominance of replicative polymerases, in early stage embryos.
POLB functions in base excision repair to fill in single-nucleotide gaps and exhibits mutation E288K associated with colon cancer. Data suggest that E288K mutant POLB exhibits faster rate of closing of fingers domain combined with slower rate of nucleotide release compared to wild-type POLB; loss of fidelity appears due to defect in interaction of E288K mutant POLB with DNA, resulting in stable, closed enzyme structure.
Unencumbered polymerase beta lyase activity in nucleosome core particles during base excision repair has been reported.
pol beta and BRCA1 appeared to have a functional interaction, observed in both DT40 and human cell lines, in protecting cells against alkylating MMS-induced cytotoxicity; but pol beta had no protective effect in the absence of BRCA1. In vivo and in vitro assays for a base excision repair role of BRCA1 were negative.
pol beta contains a specific NLS (zeige ALDH1A2 Proteine) sequence in the N-terminal lyase domain that promotes transport of the protein independent of its interaction partners. Active nuclear uptake allows development of a nuclear/cytosolic concentration gradient against a background of passive diffusion.
Data suggest that POLB activity is not essential for HIV-1 integration into human macrophages and other cells; limited cellular dNTP pools, but not POLB expression, are primary factor for HIV-1 DNA gap repair, particularly in non-dividing cells.
High DNA polymerase beta mRNA expression is associated with Graves' thyroid tissue.
Polbeta was shown to inhibit the 3'->5' exonuclease (zeige EXOSC10 Proteine) activity of APE1 (zeige APEX1 Proteine) when both enzymes were added simultaneously and to insert the correct nucleotide into the gap arising after hydrolysis of AP site clustered with the benzo[a]pyrene adducts.
Remote mutations induce functional changes in active site residues of human DNA polymerase beta.
It has been concluded based on calculations and the experimental pH profile that the most likely path for the wild-type (WT) and the D256E and D256A mutants is a proton transfer (PT) to the bulk, although the WT may also use a PT to Asp (zeige ASIP Proteine) 256.
The homozygous/heterozygous genotypes containing the African allele showed higher POLB expression than the homozygous white allele genotype (P < .001). A replication study using a GEO data set validated all 5 eQTLs and also showed a statistically significant difference in POLB expression based on genetic ancestry (P = .002).
pol beta plays an important role in bypassing a 5',8-cyclo-dA during DNA replication and repair.
we show here that heterozygosity for a Y265C mutation in Polbeta, a key polymerase in the BER pathway, is enough to significantly reduce both the number of expansions seen in paternal gametes and the extent of somatic expansion in some tissues
The aberrant DNA replication mediated by the PCNA (zeige PCNA Proteine)-DNA pol-b complex induces p53 (zeige TP53 Proteine)-dependent neuronal cell death
Y265C POLB mutation leads to several pathologies associated with SLE and short CDR3 regions during VDJ recombination in B cells.
Pol beta deficiency could enable ROS (zeige ROS1 Proteine) accumulation.
Results show that deficiency of either DNA polymerases beta or lambda or both results in a modest but significant decrease in V region somatic hypermutation (SHM (zeige CNTNAP1 Proteine)) with no effect on mutation specificity, suggesting no direct role in SHM (zeige CNTNAP1 Proteine).
Transient OGG1 (zeige OGG1 Proteine), APE1 (zeige APEX1 Proteine), PARP1 (zeige PARP1 Proteine) and Polbeta expression in an Alzheimer's disease mouse model.
Data indicate an association of ovarian stimulation with a downregulation of mRNAs encoding the base excision repair proteins APEX1 (zeige APEX1 Proteine) and POLB as well as the 5-methyl-CpG-binding domain protein MBD3 (zeige MBD3 Proteine) in individual morula embryos.
Overexpression of Pol beta could reduce oxidative damage and protect cells from hydroquinone genotoxicity.
The protein encoded by this gene is a DNA polymerase involved in base excision and repair, also called gap-filling DNA synthesis. The encoded protein, acting as a monomer, is normally found in the cytoplasm, but it translocates to the nucleus upon DNA damage. Several transcript variants of this gene exist, but the full-length nature of only one has been described to date.
DNA-directed DNA polymerase beta
, DNA polymerase beta
, polymerase (DNA directed), beta
, DNA polymerase beta-like
, DNA pol beta
, DNA polymerase beta subunit
, mutant DNA polymerase beta
, Pol beta