POLM Antibody

1. Polmu point mutations affecting 2 conserved adjacent residues located in the 8 kDa domain, G174S and R175H, limit the efficiency of accurate NHEJ by Polmu in vitro and in vivo due to decreased template dependency during NHEJ, which renders the error-rate of the mutants higher due to the ability of Polmu to randomly incorporate nucleotides at DSBs. PMID: 28973441
2. Structural accommodation of ribonucleotide incorporation by the DNA repair enzyme polymerase Mu has been described. PMID: 28911097
3. analysis of template-dependent synthesis by human polymerase mu PMID: 26240373
4. A study of how Polmu fixes and/or orients the mobile Loop1 part of the protein in accordance with the substrate on which it is polymerizing. PMID: 24878922
5. specific loop 1 residues contribute to Pol mu's unique ability to catalyze template-dependent NHEJ of DSBs with unpaired 3' ends PMID: 24487959
6. evidence suggests that Polmu could be regulated in vivo by phosphorylation of the BRCT domain (Ser12/Thr21) and of Ser372, affecting the function of loop1; Polmu's most distinctive activities would be turned off at specific cell-cycle phases (S and G2), when these functions might be harmful to the cell PMID: 23933132
7. A specific N-terminal extension of the 8 kDa domain of DNA polymerase mu is potentially implicated in the maintenance of a closed conformation throughout the catalytic cycle, and this study indicated that it could be a target of Cdk phosphorylation. PMID: 23935073
8. A physiological concentration of Mn(2+) ions did benefit Polmicro-mediated non-homologous end joining by improving the efficiency and accuracy of nucleotide insertion. PMID: 23275568
9. The study points at human Polmicro residues His(329) and Arg(387) as responsible for regulating nucleotide expansions occurring during DNA repair transactions, either promoting or blocking, respectively, iterative polymerization. PMID: 23143108
10. The results uncovered a new DNA-binding function for the BRCT domain of Polmicro and demonstrated the importance of several residues located at the primer-binding region, for both DNA-binding and polymerization activities. PMID: 23034807
11. Pol mu binds to DNA through its amino-terminal and pol beta-like regions. PMID: 22897684
12. DNA polymerase mu performs DNA synthesis at a AAF lesion PMID: 11972346
13. Association of DNA polymerase mu (pol mu) with Ku and ligase IV: role for pol mu in end-joining double-strand break repair. PMID: 12077346
14. DNA polymerase mu acts in response to several types of DNA damage with a lesion bypass mechanism PMID: 12228225
15. expression in B-cell non-Hodgkin's lymphomas PMID: 12368208
16. Pol mu's substrate specificity is similar to that of pol beta in most respects but has an approximately 1,000-fold-reduced ability to discriminate against ribonucleotides compared to pol beta PMID: 12640116
17. human DNA polymerase mu has a template-dependent, sequence-independent nucleotidyl transferase activity PMID: 14581466
18. Poliota incorporates a C opposite the gamma-HOPdG adduct with nearly the same efficiency as opposite a nonadducted G residue. The subsequent extension step is performed by Polkappa, which efficiently extends from the C incorporated opposite the adduct. PMID: 15199127
19. DNA polymerase mu has been overexpressed, purified, and its fidelity estimated for incorporation of both deoxynucleotides and ribonucleotides based on pre-steady-state kinetic data under single-turnover conditions. PMID: 15504045
20. Overexpression of DNA polymerase mu in a Burkitt's lymphoma cell line induced an increase in somatic mutations specifically targeted to G/C residues in immunoglobulin variable genes. PMID: 15520469
21. Pol mu promotes accuracy during Ig kappa recombination. PMID: 16061182
22. When the terminal deoxynucleotidyl transferase (TdT) loop1 was deleted, human Polmu lacked TdT activity but improved DNA-binding and DNA template-dependent polymerization. PMID: 16963491
23. Studies shed light on the mechanism by which a rate-limited terminal transferase activity in Polmu could regulate the balance between accuracy and necessary efficiency, providing some variability during NHEJ. PMID: 19805281

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HGNC: 9185

OMIM: 606344

KEGG: hsa:27434

STRING: 9606.ENSP00000242248

UniGene: Hs.596982