POLL or POLM extends aligned DNA DSB ends to fill gaps

Stable Identifier
Reaction [transition]
Homo sapiens
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DNA polymerases mu (POLM) and lambda (POLL) facilitate non-homologous end joining (NHEJ) of DNA double strand breaks (DSBs) by filling single strand (ss) gaps (usually 1- or 2- nucleotide gaps) present at DNA DSB ends positioned for ligation in the synaptic complex containing XRCC5:XRCC6 (Ku), PRKDC (DNA-PKcs), DCLRE1C (ARTEMIS), XRCC4:LIG4 and NHEJ1 (XLF) (Mahajan et al. 2002, Lee et al. 2004, Fan and Wu 2004, McElhinny et al. 2005, Davis et al. 2008).
Literature References
PubMed ID Title Journal Year
16061182 A gradient of template dependence defines distinct biological roles for family X polymerases in nonhomologous end joining

Havener, JM, Bebenek, K, Garcia-Diaz, M, Blanco, L, Kee, BL, Ramsden, DA, Nick McElhinny, SA, Kunkel, TA, Juárez, R

Mol. Cell 2005
18397950 End-bridging is required for pol mu to efficiently promote repair of noncomplementary ends by nonhomologous end joining

Havener, JM, Davis, BJ, Ramsden, DA

Nucleic Acids Res. 2008
12077346 Association of DNA polymerase mu (pol mu) with Ku and ligase IV: role for pol mu in end-joining double-strand break repair

Mahajan, KN, Ramsden, DA, Nick McElhinny, SA, Mitchell, BS

Mol. Cell. Biol. 2002
15451442 DNA polymerase lambda can elongate on DNA substrates mimicking non-homologous end joining and interact with XRCC4-ligase IV complex

Fan, W, Wu, X

Biochem. Biophys. Res. Commun. 2004
14561766 Implication of DNA polymerase lambda in alignment-based gap filling for nonhomologous DNA end joining in human nuclear extracts

Lee, JW, Bebenek, K, Garcia-Diaz, M, Blanco, L, Wang, Z, Kunkel, TA, Povirk, LF, Zhou, T

J. Biol. Chem. 2004
Catalyst Activity

DNA-directed DNA polymerase activity of p-T2609,S2612,T2638,T2647-PRKDC:XRCC5:XRCC6:p-S516,S645-DCLRE1C:XRCC4:LIG4:NHEJ1:POLL,POLM:Ligatable DNA DSB ends [nucleoplasm]

Orthologous Events
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