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Journal articles on the topic 'Ligase IV/XRCC4'

Author: Grafiati

Published: 6 September 2023

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1

Nick McElhinny, Stephanie A., Carey M. Snowden, Joseph McCarville, and Dale A. Ramsden. "Ku Recruits the XRCC4-Ligase IV Complex to DNA Ends." Molecular and Cellular Biology 20, no. 9 (2000): 2996–3003. http://dx.doi.org/10.1128/mcb.20.9.2996-3003.2000.

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ABSTRACT Genetic experiments have determined that Ku, XRCC4, and ligase IV are required for repair of double-strand breaks by the end-joining pathway. The last two factors form a tight complex in cells. However, ligase IV is only one of three known mammalian ligases and is intrinsically the least active in intermolecular ligation; thus, the biochemical basis for requiring this ligase has been unclear. We demonstrate here a direct physical interaction between the XRCC4-ligase IV complex and Ku. This interaction is stimulated once Ku binds to DNA ends. Since XRCC4-ligase IV alone has very low DN

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2

Wu, Peï-Yu, Philippe Frit, SriLakshmi Meesala, et al. "Structural and Functional Interaction between the Human DNA Repair Proteins DNA Ligase IV and XRCC4." Molecular and Cellular Biology 29, no. 11 (2009): 3163–72. http://dx.doi.org/10.1128/mcb.01895-08.

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ABSTRACT Nonhomologous end-joining represents the major pathway used by human cells to repair DNA double-strand breaks. It relies on the XRCC4/DNA ligase IV complex to reseal DNA strands. Here we report the high-resolution crystal structure of human XRCC4 bound to the carboxy-terminal tandem BRCT repeat of DNA ligase IV. The structure differs from the homologous Saccharomyces cerevisiae complex and reveals an extensive DNA ligase IV binding interface formed by a helix-loop-helix structure within the inter-BRCT linker region, as well as significant interactions involving the second BRCT domain,

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3

Malashetty, Vidyasagar, Audrey Au, Jose Chavez, et al. "The DNA binding domain and the C-terminal region of DNA Ligase IV specify its role in V(D)J recombination." PLOS ONE 18, no. 2 (2023): e0282236. http://dx.doi.org/10.1371/journal.pone.0282236.

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DNA Ligase IV is responsible for the repair of DNA double-strand breaks (DSB), including DSBs that are generated during V(D)J recombination. Like other DNA ligases, Ligase IV contains a catalytic core with three subdomains—the DNA binding (DBD), the nucleotidyltransferase (NTD), and the oligonucleotide/oligosaccharide-fold subdomain (OBD). Ligase IV also has a unique C-terminal region that includes two BRCT domains, a nuclear localization signal sequence and a stretch of amino acid that participate in its interaction with XRCC4. Out of the three mammalian ligases, Ligase IV is the only ligase

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4

Mahajan, Kiran N., Stephanie A. Nick McElhinny, Beverly S. Mitchell та Dale A. Ramsden. "Association of DNA Polymerase μ (pol μ) with Ku and Ligase IV: Role for pol μ in End-Joining Double-Strand Break Repair". Molecular and Cellular Biology 22, № 14 (2002): 5194–202. http://dx.doi.org/10.1128/mcb.22.14.5194-5202.2002.

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ABSTRACT Mammalian DNA polymerase μ (pol μ) is related to terminal deoxynucleotidyl transferase, but its biological role is not yet clear. We show here that after exposure of cells to ionizing radiation (IR), levels of pol μ protein increase. pol μ also forms discrete nuclear foci after IR, and these foci are largely coincident with IR-induced foci of γH2AX, a previously characterized marker of sites of DNA double-strand breaks. pol μ is thus part of the cellular response to DNA double-strand breaks. pol μ also associates in cell extracts with the nonhomologous end-joining repair factor Ku and

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5

Przewloka, Marcin R., Paige E. Pardington, Steven M. Yannone, David J. Chen, and Robert B. Cary. "In Vitro and In Vivo Interactions of DNA Ligase IV with a Subunit of the Condensin Complex." Molecular Biology of the Cell 14, no. 2 (2003): 685–97. http://dx.doi.org/10.1091/mbc.e01-11-0117.

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Several findings have revealed a likely role for DNA ligase IV, and interacting protein XRCC4, in the final steps of mammalian DNA double-strand break repair. Recent evidence suggests that the human DNA ligase IV protein plays a critical role in the maintenance of genomic stability. To identify protein–protein interactions that may shed further light on the molecular mechanisms of DSB repair and the biological roles of human DNA ligase IV, we have used the yeast two-hybrid system in conjunction with traditional biochemical methods. These efforts have resulted in the identification of a physica

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6

Francis, Dailia B., Mikhail Kozlov, Jose Chavez, et al. "DNA Ligase IV regulates XRCC4 nuclear localization." DNA Repair 21 (September 2014): 36–42. http://dx.doi.org/10.1016/j.dnarep.2014.05.010.

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7

Roy, Sunetra, Abinadabe J. de Melo, Yao Xu, et al. "XRCC4/XLF Interaction Is Variably Required for DNA Repair and Is Not Required for Ligase IV Stimulation." Molecular and Cellular Biology 35, no. 17 (2015): 3017–28. http://dx.doi.org/10.1128/mcb.01503-14.

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The classic nonhomologous end-joining (c-NHEJ) pathway is largely responsible for repairing double-strand breaks (DSBs) in mammalian cells. XLF stimulates the XRCC4/DNA ligase IV complex by an unknown mechanism. XLF interacts with XRCC4 to form filaments of alternating XRCC4 and XLF dimers that bridge DNA endsin vitro, providing a mechanism by which XLF might stimulate ligation. Here, we characterize two XLF mutants that do not interact with XRCC4 and cannot form filaments or bridge DNAin vitro. One mutant is fully sufficient in stimulating ligation by XRCC4/Lig4in vitro; the other is not. Thi

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8

Recuero-Checa, María A., Andrew S. Doré, Ernesto Arias-Palomo, et al. "Electron microscopy of Xrcc4 and the DNA ligase IV–Xrcc4 DNA repair complex." DNA Repair 8, no. 12 (2009): 1380–89. http://dx.doi.org/10.1016/j.dnarep.2009.09.007.

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9

Hayden, Patrick, Prerna Tewari, Anthony Staines, et al. "Variation in DNA Repair Genes XRCC3, XRCC4, and XRCC5 and Risk of Myeloma." Blood 108, no. 11 (2006): 3416. http://dx.doi.org/10.1182/blood.v108.11.3416.3416.

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Abstract Aberrant class switch recombination (CSR), the physiological process that regulates maturation of the antibody response, is believed to be an early event in the pathogenesis of myeloma. The genetic basis of CSR, from initiation of the DNA double-strand break through to detection and repair, has been elucidated. We hypothesised that germline polymorphisms in the genes implicated in DNA double strand break repair may contribute to susceptibility to myeloma. We therefore assessed 32 SNPs in 3 genes central to the DNA repair pathway in patients with myeloma and controls from the EpiLymph

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10

Hsu, Hsin-Ling, Steven M. Yannone, and David J. Chen. "Defining interactions between DNA-PK and ligase IV/XRCC4." DNA Repair 1, no. 3 (2002): 225–35. http://dx.doi.org/10.1016/s1568-7864(01)00018-0.

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11

Wang, Yu, Brandon J. Lamarche, and Ming-Daw Tsai. "Human DNA Ligase IV and the Ligase IV/XRCC4 Complex: Analysis of Nick Ligation Fidelity†." Biochemistry 46, no. 17 (2007): 4962–76. http://dx.doi.org/10.1021/bi0621516.

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12

Liu, Sicheng, Xunyue Liu, Radhika Pankaj Kamdar, et al. "C-terminal region of DNA ligase IV drives XRCC4/DNA ligase IV complex to chromatin." Biochemical and Biophysical Research Communications 439, no. 2 (2013): 173–78. http://dx.doi.org/10.1016/j.bbrc.2013.08.068.

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13

Reid, Dylan A., Sarah Keegan, Alejandra Leo-Macias, et al. "Organization and dynamics of the nonhomologous end-joining machinery during DNA double-strand break repair." Proceedings of the National Academy of Sciences 112, no. 20 (2015): E2575—E2584. http://dx.doi.org/10.1073/pnas.1420115112.

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Nonhomologous end-joining (NHEJ) is a major repair pathway for DNA double-strand breaks (DSBs), involving synapsis and ligation of the broken strands. We describe the use of in vivo and in vitro single-molecule methods to define the organization and interaction of NHEJ repair proteins at DSB ends. Super-resolution fluorescence microscopy allowed the precise visualization of XRCC4, XLF, and DNA ligase IV filaments adjacent to DSBs, which bridge the broken chromosome and direct rejoining. We show, by single-molecule FRET analysis of the Ku/XRCC4/XLF/DNA ligase IV NHEJ ligation complex, that end-

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14

Gu, Jiafeng, Haihui Lu, Brigette Tippin, Noriko Shimazaki, Myron F. Goodman, and Michael R. Lieber. "XRCC4:DNA ligase IV can ligate incompatible DNA ends and can ligate across gaps." EMBO Journal 26, no. 4 (2007): 1010–23. http://dx.doi.org/10.1038/sj.emboj.7601559.

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15

Gu, Jiafeng, Haihui Lu, Brigette Tippin, Noriko Shimazaki, Myron F. Goodman, and Michael R. Lieber. "XRCC4:DNA ligase IV can ligate incompatible DNA ends and can ligate across gaps." EMBO Journal 26, no. 14 (2007): 3506–7. http://dx.doi.org/10.1038/sj.emboj.7601729.

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16

Hammel, Michal, Yaping Yu, Shujuan Fang, Susan P. Lees-Miller, and John A. Tainer. "XLF Regulates Filament Architecture of the XRCC4·Ligase IV Complex." Structure 18, no. 11 (2010): 1431–42. http://dx.doi.org/10.1016/j.str.2010.09.009.

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17

Mahaney, Brandi L., Michal Hammel, Katheryn Meek, John A. Tainer, and Susan P. Lees-Miller. "XRCC4 and XLF form long helical protein filaments suitable for DNA end protection and alignment to facilitate DNA double strand break repair." Biochemistry and Cell Biology 91, no. 1 (2013): 31–41. http://dx.doi.org/10.1139/bcb-2012-0058.

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DNA double strand breaks (DSBs), induced by ionizing radiation (IR) and endogenous stress including replication failure, are the most cytotoxic form of DNA damage. In human cells, most IR-induced DSBs are repaired by the nonhomologous end joining (NHEJ) pathway. One of the most critical steps in NHEJ is ligation of DNA ends by DNA ligase IV (LIG4), which interacts with, and is stabilized by, the scaffolding protein X-ray cross-complementing gene 4 (XRCC4). XRCC4 also interacts with XRCC4-like factor (XLF, also called Cernunnos); yet, XLF has been one of the least mechanistically understood pro

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18

Riballo, Enriqueta, Lisa Woodbine, Thomas Stiff, Sarah A. Walker, Aaron A. Goodarzi, and Penny A. Jeggo. "XLF-Cernunnos promotes DNA ligase IV–XRCC4 re-adenylation following ligation." Nucleic Acids Research 37, no. 2 (2008): 482–92. http://dx.doi.org/10.1093/nar/gkn957.

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19

Jiao, Keping, Juan Qin, Yumei Zhao, and Honglian Zhang. "Genetic effects of XRCC4 and ligase IV genes on human glioma." NeuroReport 27, no. 14 (2016): 1024–30. http://dx.doi.org/10.1097/wnr.0000000000000649.

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20

Stiff, Thomas, Emma Shtivelman, Penny Jeggo, and Boris Kysela. "AHNAK interacts with the DNA ligase IV–XRCC4 complex and stimulates DNA ligase IV-mediated double-stranded ligation." DNA Repair 3, no. 3 (2004): 245–56. http://dx.doi.org/10.1016/j.dnarep.2003.11.001.

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21

Asa, Anie Day D. C., Rujira Wanotayan, Mukesh Kumar Sharma, Kaima Tsukada, Mikio Shimada, and Yoshihisa Matsumoto. "Functional analysis of XRCC4 mutations in reported microcephaly and growth defect patients in terms of radiosensitivity." Journal of Radiation Research 62, no. 3 (2021): 380–89. http://dx.doi.org/10.1093/jrr/rrab016.

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Abstract Non-homologous end joining is one of the main pathways for DNA double-strand break (DSB) repair and is also implicated in V(D)J recombination in immune system. Therefore, mutations in non-homologous end-joining (NHEJ) proteins were found to be associated with immunodeficiency in human as well as in model animals. Several human patients with mutations in XRCC4 were reported to exhibit microcephaly and growth defects, but unexpectedly showed normal immune function. Here, to evaluate the functionality of these disease-associated mutations of XRCC4 in terms of radiosensitivity, we generat

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22

Berg, Elke, Morten O. Christensen, Ilaria Dalla Rosa, et al. "XRCC4 controls nuclear import and distribution of Ligase IV and exchanges faster at damaged DNA in complex with Ligase IV." DNA Repair 10, no. 12 (2011): 1232–42. http://dx.doi.org/10.1016/j.dnarep.2011.09.012.

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23

Kusumoto, Rika, Lala Dawut, Caterina Marchetti, et al. "Werner Protein Cooperates with the XRCC4-DNA Ligase IV Complex in End-Processing†." Biochemistry 47, no. 28 (2008): 7548–56. http://dx.doi.org/10.1021/bi702325t.

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24

Critchlow, Susan E., Richard P. Bowater, and Stephen P. Jackson. "Mammalian DNA double-strand break repair protein XRCC4 interacts with DNA ligase IV." Current Biology 7, no. 8 (1997): 588–98. http://dx.doi.org/10.1016/s0960-9822(06)00258-2.

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25

Fukuchi, Mikoto, Rujira Wanotayan, Sicheng Liu, Shoji Imamichi, Mukesh Kumar Sharma, and Yoshihisa Matsumoto. "Lysine 271 but not lysine 210 of XRCC4 is required for the nuclear localization of XRCC4 and DNA ligase IV." Biochemical and Biophysical Research Communications 461, no. 4 (2015): 687–94. http://dx.doi.org/10.1016/j.bbrc.2015.04.093.

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26

Ochi, Takashi, Bancinyane Lynn Sibanda, Qian Wu, Dimitri Y. Chirgadze, Victor M. Bolanos-Garcia, and Tom L. Blundell. "Structural Biology of DNA Repair: Spatial Organisation of the Multicomponent Complexes of Nonhomologous End Joining." Journal of Nucleic Acids 2010 (2010): 1–19. http://dx.doi.org/10.4061/2010/621695.

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Nonhomologous end joining (NHEJ) plays a major role in double-strand break DNA repair, which involves a series of steps mediated by multiprotein complexes. A ring-shaped Ku70/Ku80 heterodimer forms first at broken DNA ends, DNA-dependent protein kinase catalytic subunit (DNA-PKcs) binds to mediate synapsis and nucleases process DNA overhangs. DNA ligase IV (LigIV) is recruited as a complex with XRCC4 for ligation, with XLF/Cernunnos, playing a role in enhancing activity of LigIV. We describe how a combination of methods—X-ray crystallography, electron microscopy and small angle X-ray scatterin

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27

Malivert, Laurent, Isabelle Callebaut, Paola Rivera-Munoz, et al. "The C-Terminal Domain of Cernunnos/XLF Is Dispensable for DNA Repair In Vivo." Molecular and Cellular Biology 29, no. 5 (2008): 1116–22. http://dx.doi.org/10.1128/mcb.01521-08.

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ABSTRACT The core nonhomologous end-joining DNA repair pathway is composed of seven factors: Ku70, Ku80, DNA-PKcs, Artemis, XRCC4 (X4), DNA ligase IV (L4), and Cernunnos/XLF (Cernunnos). Although Cernunnos and X4 are structurally related and participate in the same complex together with L4, they have distinct functions during DNA repair. L4 relies on X4 but not on Cernunnos for its stability, and L4 is required for optimal interaction of Cernunnos with X4. We demonstrate here, using in vitro-generated Cernunnos mutants and a series of functional assays in vivo, that the C-terminal region of Ce

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28

Grawunder, Ulf, Matthias Wilm, Xiantuo Wu, et al. "Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells." Nature 388, no. 6641 (1997): 492–95. http://dx.doi.org/10.1038/41358.

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29

Bryans, Margaret, Mary Carmen Valenzano, and Thomas D. Stamato. "Absence of DNA ligase IV protein in XR-1 cells: evidence for stabilization by XRCC4." Mutation Research/DNA Repair 433, no. 1 (1999): 53–58. http://dx.doi.org/10.1016/s0921-8777(98)00063-9.

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30

Ahnesorg, Peter, Philippa Smith, and Stephen P. Jackson. "XLF Interacts with the XRCC4-DNA Ligase IV Complex to Promote DNA Nonhomologous End-Joining." Cell 124, no. 2 (2006): 301–13. http://dx.doi.org/10.1016/j.cell.2005.12.031.

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31

Sallmyr, Annahita, та Feyruz V. Rassool. "Up-Regulated WRN and DNA Ligase IIIα Are Involved in Alternative NHEJ Repair Pathway of DNA Double Strand Breaks (DSB) in Chronic Myeloid Leukemia (CML)." Blood 110, № 11 (2007): 1016. http://dx.doi.org/10.1182/blood.v110.11.1016.1016.

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Abstract The oncogenic BCR-ABL in CML produces increased reactive oxygen species (ROS) leading to DSB and aberrant repair. We have previously shown that CML cells demonstrate an increased frequency of errors of non homologous end-joining (NHEJ). DSB are repaired by two major pathways, homologous recombination (HR) and NHEJ, the dominant pathway in eukaryotic cells, also known as DNA-PK dependent NHEJ (D-NHEJ). Recent reports have identified alternative or “back-up” NHEJ pathways (B-NHEJ) that are highly error-prone, and may explain the altered DSB repair reported in CML. To determine the mecha

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32

Liang, Zhuoyi, Vipul Kumar, Marie Le Bouteiller, et al. "Ku70 suppresses alternative end joining in G1-arrested progenitor B cells." Proceedings of the National Academy of Sciences 118, no. 21 (2021): e2103630118. http://dx.doi.org/10.1073/pnas.2103630118.

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Classical nonhomologous end joining (C-NHEJ) repairs DNA double-strand breaks (DSBs) throughout interphase but predominates in G1 phase when homologous recombination is unavailable. Complexes containing the Ku70/80 (“Ku”) and XRCC4/ligase IV (Lig4) core C-NHEJ factors are required, respectively, for sensing and joining DSBs. While XRCC4/Lig4 are absolutely required for joining RAG1/2 endonuclease (“RAG”)-initiated DSBs during V(D)J recombination in G1-phase progenitor lymphocytes, cycling cells deficient for XRCC4/Lig4 also can join chromosomal DSBs by alternative end-joining (A-EJ) pathways.

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33

Mahaney, Brandi L., Katheryn Meek, and Susan P. Lees-Miller. "Repair of ionizing radiation-induced DNA double-strand breaks by non-homologous end-joining." Biochemical Journal 417, no. 3 (2009): 639–50. http://dx.doi.org/10.1042/bj20080413.

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DNA DSBs (double-strand breaks) are considered the most cytotoxic type of DNA lesion. They can be introduced by external sources such as IR (ionizing radiation), by chemotherapeutic drugs such as topoisomerase poisons and by normal biological processes such as V(D)J recombination. If left unrepaired, DSBs can cause cell death. If misrepaired, DSBs may lead to chromosomal translocations and genomic instability. One of the major pathways for the repair of IR-induced DSBs in mammalian cells is NHEJ (non-homologous end-joining). The main proteins required for NHEJ in mammalian cells are the Ku het

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34

Lu, Haihui, Ulrich Pannicke, Klaus Schwarz, and Michael R. Lieber. "Length-dependent Binding of Human XLF to DNA and Stimulation of XRCC4·DNA Ligase IV Activity." Journal of Biological Chemistry 282, no. 15 (2007): 11155–62. http://dx.doi.org/10.1074/jbc.m609904200.

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35

Budman, Joe, Sunny A. Kim, and Gilbert Chu. "Processing of DNA for Nonhomologous End-joining Is Controlled by Kinase Activity and XRCC4/Ligase IV." Journal of Biological Chemistry 282, no. 16 (2007): 11950–59. http://dx.doi.org/10.1074/jbc.m610058200.

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36

Doré, Andrew S., Nicholas Furnham, Owen R. Davies, et al. "Structure of an Xrcc4–DNA ligase IV yeast ortholog complex reveals a novel BRCT interaction mode." DNA Repair 5, no. 3 (2006): 362–68. http://dx.doi.org/10.1016/j.dnarep.2005.11.004.

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37

Gerodimos, Christina A., Howard H. Y. Chang, Go Watanabe, and Michael R. Lieber. "Effects of DNA end configuration on XRCC4-DNA ligase IV and its stimulation of Artemis activity." Journal of Biological Chemistry 292, no. 34 (2017): 13914–24. http://dx.doi.org/10.1074/jbc.m117.798850.

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38

Koch, Christine Anne, Roger Agyei, Sarah Galicia, et al. "Xrcc4 physically links DNA end processing by polynucleotide kinase to DNA ligation by DNA ligase IV." EMBO Journal 23, no. 19 (2004): 3874–85. http://dx.doi.org/10.1038/sj.emboj.7600375.

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39

Chen, Ling, Kelly Trujillo, Patrick Sung, and Alan E. Tomkinson. "Interactions of the DNA Ligase IV-XRCC4 Complex with DNA Ends and the DNA-dependent Protein Kinase." Journal of Biological Chemistry 275, no. 34 (2000): 26196–205. http://dx.doi.org/10.1074/jbc.m000491200.

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40

Aceytuno, D., C. G. Piett, Z. Havali-Shahriari, et al. "Clinical dysregulation of DNA repair by the polynucleotide kinase/phosphatase-XRCC4-DNA ligase IV in neurological disease." Annals of Oncology 28 (September 2017): v17. http://dx.doi.org/10.1093/annonc/mdx361.058.

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41

Muylaert, Isabella, and Per Elias. "Knockdown of DNA Ligase IV/XRCC4 by RNA Interference Inhibits Herpes Simplex Virus Type I DNA Replication." Journal of Biological Chemistry 282, no. 15 (2007): 10865–72. http://dx.doi.org/10.1074/jbc.m611834200.

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42

Grawunder, Ulf, David Zimmer, and Michael R. Lieber. "DNA ligase IV binds to XRCC4 via a motif located between rather than within its BRCT domains." Current Biology 8, no. 15 (1998): 873–79. http://dx.doi.org/10.1016/s0960-9822(07)00349-1.

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43

Jayaram, Sumithra, Timra Gilson, Elana S. Ehrlich, Xiao-Fang Yu, Gary Ketner, and Les Hanakahi. "E1B 55k-independent dissociation of the DNA ligase IV/XRCC4 complex by E4 34k during adenovirus infection." Virology 382, no. 2 (2008): 163–70. http://dx.doi.org/10.1016/j.virol.2008.08.045.

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44

Simsek, Deniz, and Maria Jasin. "Alternative end-joining is suppressed by the canonical NHEJ component Xrcc4–ligase IV during chromosomal translocation formation." Nature Structural & Molecular Biology 17, no. 4 (2010): 410–16. http://dx.doi.org/10.1038/nsmb.1773.

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45

McFadden, Meghan J., Wilson K. Y. Lee, John D. Brennan, and Murray S. Junop. "Delineation of key XRCC4/Ligase IV interfaces for targeted disruption of non-homologous end joining DNA repair." Proteins: Structure, Function, and Bioinformatics 82, no. 2 (2013): 187–94. http://dx.doi.org/10.1002/prot.24349.

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46

Jayaram, Sumithra, Gary Ketner, Noritaka Adachi, and Les A. Hanakahi. "Loss of DNA ligase IV prevents recognition of DNA by double-strand break repair proteins XRCC4 and XLF." Nucleic Acids Research 36, no. 18 (2008): 5773–86. http://dx.doi.org/10.1093/nar/gkn552.

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47

Costantini, Silvia, Lisa Woodbine, Lucia Andreoli, Penny A. Jeggo, and Alessandro Vindigni. "Interaction of the Ku heterodimer with the DNA ligase IV/Xrcc4 complex and its regulation by DNA-PK." DNA Repair 6, no. 6 (2007): 712–22. http://dx.doi.org/10.1016/j.dnarep.2006.12.007.

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48

Chiruvella, Kishore K., Brian M. Renard, Shanda R. Birkeland, Sham Sunder, Zhuobin Liang, and Thomas E. Wilson. "Yeast DNA ligase IV mutations reveal a nonhomologous end joining function of BRCT1 distinct from XRCC4/Lif1 binding." DNA Repair 24 (December 2014): 37–45. http://dx.doi.org/10.1016/j.dnarep.2014.10.003.

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49

Modesti, Mauro, Murray S. Junop, Rodolfo Ghirlando, et al. "Tetramerization and DNA Ligase IV Interaction of the DNA Double-strand Break Repair Protein XRCC4 are Mutually Exclusive." Journal of Molecular Biology 334, no. 2 (2003): 215–28. http://dx.doi.org/10.1016/j.jmb.2003.09.031.

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50

Yoder, Kristine E., and Frederic D. Bushman. "Repair of Gaps in Retroviral DNA Integration Intermediates." Journal of Virology 74, no. 23 (2000): 11191–200. http://dx.doi.org/10.1128/jvi.74.23.11191-11200.2000.

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ABSTRACT Diverse mobile DNA elements are believed to pirate host cell enzymes to complete DNA transfer. Prominent examples are provided by retroviral cDNA integration and transposon insertion. These reactions initially involve the attachment of each element 3′ DNA end to staggered sites in the host DNA by element-encoded integrase or transposase enzymes. Unfolding of such intermediates yields DNA gaps at each junction. It has been widely assumed that host DNA repair enzymes complete attachment of the remaining DNA ends, but the enzymes involved have not been identified for any system. We have

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