| DNA Polymerase and dRP-lyase activities of polymorphic variants of human Pol iota. | DNA Polymerase and dRP-lyase activities of polymorphic variants of human Pol ι.
Shilkin ES, Gromova AS, Smal MP, Makarova AV. | 11/6/2021 |
| Mechanism of genome instability mediated by human DNA polymerase mu misincorporation. | Mechanism of genome instability mediated by human DNA polymerase mu misincorporation.
Guo M, Wang Y, Tang Y, Chen Z, Hou J, Dai J, Wang Y, Wang L, Xu H, Tian B, Hua Y, Zhao Y., Free PMC Article | 07/10/2021 |
| DNA polymerase mu: An inflexible scaffold for substrate flexibility. | DNA polymerase mu: An inflexible scaffold for substrate flexibility.
Kaminski AM, Bebenek K, Pedersen LC, Kunkel TA., Free PMC Article | 03/28/2021 |
| pol mu-mediated deoxyguanosine triphosphate mismatch insertion opposite template base T coupled with ligation could be a feature of mutation prone nonhomologous end joining during double-strand break repair. | Pol μ dGTP mismatch insertion opposite T coupled with ligation reveals promutagenic DNA repair intermediate.
Çağlayan M, Wilson SH., Free PMC Article | 01/12/2019 |
| 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. | Polμ tumor variants decrease the efficiency and accuracy of NHEJ.
Sastre-Moreno G, Pryor JM, Díaz-Talavera A, Ruiz JF, Ramsden DA, Blanco L., Free PMC Article | 12/2/2017 |
| Structural accommodation of ribonucleotide incorporation by the DNA repair enzyme polymerase Mu has been described. | Structural accommodation of ribonucleotide incorporation by the DNA repair enzyme polymerase Mu.
Moon AF, Pryor JM, Ramsden DA, Kunkel TA, Bebenek K, Pedersen LC., Free PMC Article | 10/14/2017 |
| analysis of template-dependent synthesis by human polymerase mu | Creative template-dependent synthesis by human polymerase mu.
Moon AF, Gosavi RA, Kunkel TA, Pedersen LC, Bebenek K., Free PMC Article | 04/30/2016 |
| 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. | Decision-making during NHEJ: a network of interactions in human Polμ implicated in substrate recognition and end-bridging.
Martin MJ, Blanco L., Free PMC Article | 09/6/2014 |
| specific loop 1 residues contribute to Pol mu's unique ability to catalyze template-dependent NHEJ of DSBs with unpaired 3' ends | Sustained active site rigidity during synthesis by human DNA polymerase μ.
Moon AF, Pryor JM, Ramsden DA, Kunkel TA, Bebenek K, Pedersen LC., Free PMC Article | 05/3/2014 |
| 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 | The BRCT domain and the specific loop 1 of human Polμ are targets of Cdk2/cyclin A phosphorylation.
Esteban V, Martin MJ, Blanco L. | 01/11/2014 |
| 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. | A specific N-terminal extension of the 8 kDa domain is required for DNA end-bridging by human Polμ and Polλ.
Martin MJ, Garcia-Ortiz MV, Gomez-Bedoya A, Esteban V, Guerra S, Blanco L., Free PMC Article | 01/4/2014 |
| A physiological concentration of Mn(2+) ions did benefit Polmicro-mediated non-homologous end joining by improving the efficiency and accuracy of nucleotide insertion. | Ribonucleotides and manganese ions improve non-homologous end joining by human Polμ.
Martin MJ, Garcia-Ortiz MV, Esteban V, Blanco L., Free PMC Article | 05/11/2013 |
| 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. | DNA expansions generated by human Polμ on iterative sequences.
Aza A, Martin MJ, Juarez R, Blanco L, Terrados G., Free PMC Article | 03/23/2013 |
| 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. | DNA-binding determinants promoting NHEJ by human Polμ.
Martin MJ, Juarez R, Blanco L., Free PMC Article | 02/23/2013 |
| Pol mu binds to DNA through its amino-terminal and pol beta-like regions. | BRCT domain of DNA polymerase μ has DNA-binding activity and promotes the DNA polymerization activity.
Matsumoto T, Go K, Hyodo M, Koiwai K, Maezawa S, Hayano T, Suzuki M, Koiwai O. | 01/5/2013 |
| 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. | Limited terminal transferase in human DNA polymerase mu defines the required balance between accuracy and efficiency in NHEJ.
Andrade P, Martín MJ, Juárez R, López de Saro F, Blanco L., Free PMC Article | 01/21/2010 |
| Observational study of gene-disease association, gene-gene interaction, and gene-environment interaction. (HuGE Navigator) | Genetic polymorphisms in 85 DNA repair genes and bladder cancer risk.
Michiels S, Laplanche A, Boulet T, Dessen P, Guillonneau B, Méjean A, Desgrandchamps F, Lathrop M, Sarasin A, Benhamou S. | 03/25/2009 |
| DNA polymerase mu performs DNA synthesis at a AAF lesion | Human DNA polymerase mu (Pol mu) exhibits an unusual replication slippage ability at AAF lesion.
Duvauchelle JB, Blanco L, Fuchs RP, Cordonnier AM., Free PMC Article | 01/21/2010 |
| Pol mu promotes accuracy during Ig kappa recombination. | A gradient of template dependence defines distinct biological roles for family X polymerases in nonhomologous end joining.
Nick McElhinny SA, Havener JM, Garcia-Diaz M, Juárez R, Bebenek K, Kee BL, Blanco L, Kunkel TA, Ramsden DA. | 01/21/2010 |
| DNA polymerase mu acts in response to several types of DNA damage with a lesion bypass mechanism | Lesion bypass activities of human DNA polymerase mu.
Zhang Y, Wu X, Guo D, Rechkoblit O, Taylor JS, Geacintov NE, Wang Z. | 01/21/2010 |
| expression in B-cell non-Hodgkin's lymphomas | DNA polymerase mu gene expression in B-cell non-Hodgkin's lymphomas: an analysis utilizing in situ hybridization.
Chiu A, Pan L, Li Z, Ely S, Chadburn A, Knowles DM., Free PMC Article | 01/21/2010 |
| 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 | Polymerase mu is a DNA-directed DNA/RNA polymerase.
Nick McElhinny SA, Ramsden DA., Free PMC Article | 01/21/2010 |
| role in DNA repair | [Expression and function of terminal deoxynucleotidyl-transferase and discovery of novel DNA polymerase mu].
Shimazaki N, Fujita K, Koiwai O. | 01/21/2010 |
| 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. | Overexpression of human DNA polymerase mu (Pol mu) in a Burkitt's lymphoma cell line affects the somatic hypermutation rate.
Ruiz JF, Lucas D, García-Palomero E, Saez AI, González MA, Piris MA, Bernad A, Blanco L., Free PMC Article | 01/21/2010 |
| human DNA polymerase mu has a template-dependent, sequence-independent nucleotidyl transferase activity | Lesion bypass by human DNA polymerase mu reveals a template-dependent, sequence-independent nucleotidyl transferase activity.
Covo S, Blanco L, Livneh Z. | 01/21/2010 |