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Polmicro expression was detected not only in pro- and mesonephros, the major sites for B-lymphocyte (show AKAP17A Proteins) development, but also in ovary and testis and in all tissue preparations to a low extent.
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.
Structural accommodation of ribonucleotide incorporation by the DNA repair enzyme polymerase Mu has been described.
analysis of template-dependent synthesis by human polymerase mu
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.
specific loop 1 residues contribute to Pol mu's unique ability to catalyze template-dependent NHEJ of DSBs with unpaired 3' ends
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
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 (show CDK4 Proteins) phosphorylation.
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.
Pol mu binds to DNA through its amino-terminal and pol beta (show POLB Proteins)-like regions.
DNA polymerase mu performs DNA synthesis at a AAF lesion
A role for PolMU in the prevention of sarcomagenesis on a murine P53 (show TP53 Proteins)-deficient background was identified.
Pol mu and Pol lambda (show POLL Proteins) play a key role in conferring on NHEJ the flexibility required for accurate and efficient repair
Polmu deficiency activates transcriptional networks that reduce constitutive apoptosis, leading to enhanced liver repair at old age.
DNA polymerase mu has a role in decreased learning and brain long-term potentiation in aged mice
These data point to a critical role for pol mu as a global repair player that increases the efficiency and the fidelity of non-homologous end-joining.
A series of molecular-dynamics simulations with and without the incoming nucleotide in various forms, including mutant systems, based on pol mu's crystal ternary structure, were analyzed.
Pol mu is not required for normal Ig gene hypermutation.
Pol mu promotes accuracy during Ig kappa recombination.
third hypervariable region assumes for each immunoglobulin chain, with pol lambda (show POLL Proteins) maintaining a large heavy chain junctional heterogeneity and pol mu ensuring a restricted light chain junctional variability
The crystal structure of the polymerase domain of murine Pol mu bound to gapped DNA with a correct dNTP at the active site reveals substrate interactions with side chains in Pol mu that differ from other family X members.
Gap-filling polymerase involved in repair of DNA double- strand breaks by non-homologous end joining (NHEJ). Participates in immunoglobulin (Ig) light chain gene rearrangement in V(D)J recombination.
DNA polymerase mu
, DNA-directed DNA polymerase mu
, DNA-directed DNA/RNA polymerase mu
, polymerase (DNA directed), mu
, DNA polymerase mu-like
, Pol iota
, polymerase (DNA-directed), mu
, terminal transferase
, pol Mu