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. 1998 Apr 1;17(7):2122–2136. doi: 10.1093/emboj/17.7.2122

Transposase makes critical contacts with, and is stimulated by, single-stranded DNA at the P element termini in vitro.

E L Beall 1, D C Rio 1
PMCID: PMC1170556  PMID: 9524133

Abstract

P elements transpose by a cut-and-paste mechanism. Donor DNA cleavage mediated by transposase generates 17 nucleotide (nt) 3' single-strand extensions at the P element termini which, when present on oligonucleotide substrates, stimulate both the strand-transfer and disintegration reactions in vitro. A significant amount of the strand-transfer products are the result of double-ended integration. Chemical DNA modification-interference experiments indicate that during the strand-transfer reaction, P element transposase contacts regions of the substrate DNA that include the transposase binding site and the duplex portion of the 31 bp inverted repeat, as well as regions of the terminal 17 nt single-stranded DNA. Together these data suggest that the P element transposase protein contains two DNA-binding sites and that the active oligomeric form of the transposase protein is at least a dimer.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Aldaz H., Schuster E., Baker T. A. The interwoven architecture of the Mu transposase couples DNA synapsis to catalysis. Cell. 1996 Apr 19;85(2):257–269. doi: 10.1016/s0092-8674(00)81102-2. [DOI] [PubMed] [Google Scholar]
  2. Bainton R., Gamas P., Craig N. L. Tn7 transposition in vitro proceeds through an excised transposon intermediate generated by staggered breaks in DNA. Cell. 1991 May 31;65(5):805–816. doi: 10.1016/0092-8674(91)90388-f. [DOI] [PubMed] [Google Scholar]
  3. Baker T. A., Luo L. Identification of residues in the Mu transposase essential for catalysis. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6654–6658. doi: 10.1073/pnas.91.14.6654. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Beall E. L., Admon A., Rio D. C. A Drosophila protein homologous to the human p70 Ku autoimmune antigen interacts with the P transposable element inverted repeats. Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12681–12685. doi: 10.1073/pnas.91.26.12681. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Beall E. L., Rio D. C. Drosophila IRBP/Ku p70 corresponds to the mutagen-sensitive mus309 gene and is involved in P-element excision in vivo. Genes Dev. 1996 Apr 15;10(8):921–933. doi: 10.1101/gad.10.8.921. [DOI] [PubMed] [Google Scholar]
  6. Beall E. L., Rio D. C. Drosophila P-element transposase is a novel site-specific endonuclease. Genes Dev. 1997 Aug 15;11(16):2137–2151. doi: 10.1101/gad.11.16.2137. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Benjamin H. W., Kleckner N. Excision of Tn10 from the donor site during transposition occurs by flush double-strand cleavages at the transposon termini. Proc Natl Acad Sci U S A. 1992 May 15;89(10):4648–4652. doi: 10.1073/pnas.89.10.4648. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Blunt T., Finnie N. J., Taccioli G. E., Smith G. C., Demengeot J., Gottlieb T. M., Mizuta R., Varghese A. J., Alt F. W., Jeggo P. A. Defective DNA-dependent protein kinase activity is linked to V(D)J recombination and DNA repair defects associated with the murine scid mutation. Cell. 1995 Mar 10;80(5):813–823. doi: 10.1016/0092-8674(95)90360-7. [DOI] [PubMed] [Google Scholar]
  9. Bolland S., Kleckner N. The three chemical steps of Tn10/IS10 transposition involve repeated utilization of a single active site. Cell. 1996 Jan 26;84(2):223–233. doi: 10.1016/s0092-8674(00)80977-0. [DOI] [PubMed] [Google Scholar]
  10. Boubnov N. V., Hall K. T., Wills Z., Lee S. E., He D. M., Benjamin D. M., Pulaski C. R., Band H., Reeves W., Hendrickson E. A. Complementation of the ionizing radiation sensitivity, DNA end binding, and V(D)J recombination defects of double-strand break repair mutants by the p86 Ku autoantigen. Proc Natl Acad Sci U S A. 1995 Jan 31;92(3):890–894. doi: 10.1073/pnas.92.3.890. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Brunelle A., Schleif R. F. Missing contact probing of DNA-protein interactions. Proc Natl Acad Sci U S A. 1987 Oct;84(19):6673–6676. doi: 10.1073/pnas.84.19.6673. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Bujacz G., Jaskólski M., Alexandratos J., Wlodawer A., Merkel G., Katz R. A., Skalka A. M. High-resolution structure of the catalytic domain of avian sarcoma virus integrase. J Mol Biol. 1995 Oct 20;253(2):333–346. doi: 10.1006/jmbi.1995.0556. [DOI] [PubMed] [Google Scholar]
  13. Bujacz G., Jaskólski M., Alexandratos J., Wlodawer A., Merkel G., Katz R. A., Skalka A. M. The catalytic domain of avian sarcoma virus integrase: conformation of the active-site residues in the presence of divalent cations. Structure. 1996 Jan 15;4(1):89–96. doi: 10.1016/s0969-2126(96)00012-3. [DOI] [PubMed] [Google Scholar]
  14. Bushman F. D., Craigie R. Integration of human immunodeficiency virus DNA: adduct interference analysis of required DNA sites. Proc Natl Acad Sci U S A. 1992 Apr 15;89(8):3458–3462. doi: 10.1073/pnas.89.8.3458. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Cao Q. P., Pitt S., Leszyk J., Baril E. F. DNA-dependent ATPase from HeLa cells is related to human Ku autoantigen. Biochemistry. 1994 Jul 19;33(28):8548–8557. doi: 10.1021/bi00194a021. [DOI] [PubMed] [Google Scholar]
  16. Cech T. R. The chemistry of self-splicing RNA and RNA enzymes. Science. 1987 Jun 19;236(4808):1532–1539. doi: 10.1126/science.2438771. [DOI] [PubMed] [Google Scholar]
  17. Chen J. L., Attardi L. D., Verrijzer C. P., Yokomori K., Tjian R. Assembly of recombinant TFIID reveals differential coactivator requirements for distinct transcriptional activators. Cell. 1994 Oct 7;79(1):93–105. doi: 10.1016/0092-8674(94)90403-0. [DOI] [PubMed] [Google Scholar]
  18. Chow S. A., Brown P. O. Juxtaposition of two viral DNA ends in a bimolecular disintegration reaction mediated by multimers of human immunodeficiency virus type 1 or murine leukemia virus integrase. J Virol. 1994 Dec;68(12):7869–7878. doi: 10.1128/jvi.68.12.7869-7878.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Chow S. A., Brown P. O. Substrate features important for recognition and catalysis by human immunodeficiency virus type 1 integrase identified by using novel DNA substrates. J Virol. 1994 Jun;68(6):3896–3907. doi: 10.1128/jvi.68.6.3896-3907.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Chow S. A., Vincent K. A., Ellison V., Brown P. O. Reversal of integration and DNA splicing mediated by integrase of human immunodeficiency virus. Science. 1992 Feb 7;255(5045):723–726. doi: 10.1126/science.1738845. [DOI] [PubMed] [Google Scholar]
  21. Craig N. L. Target site selection in transposition. Annu Rev Biochem. 1997;66:437–474. doi: 10.1146/annurev.biochem.66.1.437. [DOI] [PubMed] [Google Scholar]
  22. Craig N. L. Unity in transposition reactions. Science. 1995 Oct 13;270(5234):253–254. doi: 10.1126/science.270.5234.253. [DOI] [PubMed] [Google Scholar]
  23. Craigie R., Mizuuchi K. Transposition of Mu DNA: joining of Mu to target DNA can be uncoupled from cleavage at the ends of Mu. Cell. 1987 Nov 6;51(3):493–501. doi: 10.1016/0092-8674(87)90645-3. [DOI] [PubMed] [Google Scholar]
  24. Cuomo C. A., Mundy C. L., Oettinger M. A. DNA sequence and structure requirements for cleavage of V(D)J recombination signal sequences. Mol Cell Biol. 1996 Oct;16(10):5683–5690. doi: 10.1128/mcb.16.10.5683. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Dyda F., Hickman A. B., Jenkins T. M., Engelman A., Craigie R., Davies D. R. Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases. Science. 1994 Dec 23;266(5193):1981–1986. doi: 10.1126/science.7801124. [DOI] [PubMed] [Google Scholar]
  26. Ellison V., Brown P. O. A stable complex between integrase and viral DNA ends mediates human immunodeficiency virus integration in vitro. Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):7316–7320. doi: 10.1073/pnas.91.15.7316. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Ellison V., Gerton J., Vincent K. A., Brown P. O. An essential interaction between distinct domains of HIV-1 integrase mediates assembly of the active multimer. J Biol Chem. 1995 Feb 17;270(7):3320–3326. doi: 10.1074/jbc.270.7.3320. [DOI] [PubMed] [Google Scholar]
  28. Engelman A., Bushman F. D., Craigie R. Identification of discrete functional domains of HIV-1 integrase and their organization within an active multimeric complex. EMBO J. 1993 Aug;12(8):3269–3275. doi: 10.1002/j.1460-2075.1993.tb05996.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Engels W. R., Johnson-Schlitz D. M., Eggleston W. B., Sved J. High-frequency P element loss in Drosophila is homolog dependent. Cell. 1990 Aug 10;62(3):515–525. doi: 10.1016/0092-8674(90)90016-8. [DOI] [PubMed] [Google Scholar]
  30. Errami A., Smider V., Rathmell W. K., He D. M., Hendrickson E. A., Zdzienicka M. Z., Chu G. Ku86 defines the genetic defect and restores X-ray resistance and V(D)J recombination to complementation group 5 hamster cell mutants. Mol Cell Biol. 1996 Apr;16(4):1519–1526. doi: 10.1128/mcb.16.4.1519. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Gary P. A., Biery M. C., Bainton R. J., Craig N. L. Multiple DNA processing reactions underlie Tn7 transposition. J Mol Biol. 1996 Mar 29;257(2):301–316. doi: 10.1006/jmbi.1996.0164. [DOI] [PubMed] [Google Scholar]
  32. Griffith A. J., Blier P. R., Mimori T., Hardin J. A. Ku polypeptides synthesized in vitro assemble into complexes which recognize ends of double-stranded DNA. J Biol Chem. 1992 Jan 5;267(1):331–338. [PubMed] [Google Scholar]
  33. Gu Y., Jin S., Gao Y., Weaver D. T., Alt F. W. Ku70-deficient embryonic stem cells have increased ionizing radiosensitivity, defective DNA end-binding activity, and inability to support V(D)J recombination. Proc Natl Acad Sci U S A. 1997 Jul 22;94(15):8076–8081. doi: 10.1073/pnas.94.15.8076. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Hegde R. S., Grossman S. R., Laimins L. A., Sigler P. B. Crystal structure at 1.7 A of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target. Nature. 1992 Oct 8;359(6395):505–512. doi: 10.1038/359505a0. [DOI] [PubMed] [Google Scholar]
  35. Hochschild A., Ptashne M. Cooperative binding of lambda repressors to sites separated by integral turns of the DNA helix. Cell. 1986 Mar 14;44(5):681–687. doi: 10.1016/0092-8674(86)90833-0. [DOI] [PubMed] [Google Scholar]
  36. Jackson S. P. The recognition of DNA damage. Curr Opin Genet Dev. 1996 Feb;6(1):19–25. doi: 10.1016/s0959-437x(96)90005-2. [DOI] [PubMed] [Google Scholar]
  37. Katz R. A., Skalka A. M. The retroviral enzymes. Annu Rev Biochem. 1994;63:133–173. doi: 10.1146/annurev.bi.63.070194.001025. [DOI] [PubMed] [Google Scholar]
  38. Kaufman P. D., Doll R. F., Rio D. C. Drosophila P element transposase recognizes internal P element DNA sequences. Cell. 1989 Oct 20;59(2):359–371. doi: 10.1016/0092-8674(89)90297-3. [DOI] [PubMed] [Google Scholar]
  39. Kaufman P. D., Rio D. C. P element transposition in vitro proceeds by a cut-and-paste mechanism and uses GTP as a cofactor. Cell. 1992 Apr 3;69(1):27–39. doi: 10.1016/0092-8674(92)90116-t. [DOI] [PubMed] [Google Scholar]
  40. Kirchgessner C. U., Patil C. K., Evans J. W., Cuomo C. A., Fried L. M., Carter T., Oettinger M. A., Brown J. M. DNA-dependent kinase (p350) as a candidate gene for the murine SCID defect. Science. 1995 Feb 24;267(5201):1178–1183. doi: 10.1126/science.7855601. [DOI] [PubMed] [Google Scholar]
  41. Kulkosky J., Jones K. S., Katz R. A., Mack J. P., Skalka A. M. Residues critical for retroviral integrative recombination in a region that is highly conserved among retroviral/retrotransposon integrases and bacterial insertion sequence transposases. Mol Cell Biol. 1992 May;12(5):2331–2338. doi: 10.1128/mcb.12.5.2331. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Lee C. C., Mul Y. M., Rio D. C. The Drosophila P-element KP repressor protein dimerizes and interacts with multiple sites on P-element DNA. Mol Cell Biol. 1996 Oct;16(10):5616–5622. doi: 10.1128/mcb.16.10.5616. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Li R., Knight J., Bream G., Stenlund A., Botchan M. Specific recognition nucleotides and their DNA context determine the affinity of E2 protein for 17 binding sites in the BPV-1 genome. Genes Dev. 1989 Apr;3(4):510–526. doi: 10.1101/gad.3.4.510. [DOI] [PubMed] [Google Scholar]
  44. Mimori T., Hardin J. A. Mechanism of interaction between Ku protein and DNA. J Biol Chem. 1986 Aug 5;261(22):10375–10379. [PubMed] [Google Scholar]
  45. Mizuuchi K., Adzuma K. Inversion of the phosphate chirality at the target site of Mu DNA strand transfer: evidence for a one-step transesterification mechanism. Cell. 1991 Jul 12;66(1):129–140. doi: 10.1016/0092-8674(91)90145-o. [DOI] [PubMed] [Google Scholar]
  46. Mizuuchi K. Polynucleotidyl transfer reactions in transpositional DNA recombination. J Biol Chem. 1992 Oct 25;267(30):21273–21276. [PubMed] [Google Scholar]
  47. Mizuuchi K. Transpositional recombination: mechanistic insights from studies of mu and other elements. Annu Rev Biochem. 1992;61:1011–1051. doi: 10.1146/annurev.bi.61.070192.005051. [DOI] [PubMed] [Google Scholar]
  48. Mizuuchi M., Baker T. A., Mizuuchi K. DNase protection analysis of the stable synaptic complexes involved in Mu transposition. Proc Natl Acad Sci U S A. 1991 Oct 15;88(20):9031–9035. doi: 10.1073/pnas.88.20.9031. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Mizuuchi M., Mizuuchi K. Efficient Mu transposition requires interaction of transposase with a DNA sequence at the Mu operator: implications for regulation. Cell. 1989 Jul 28;58(2):399–408. doi: 10.1016/0092-8674(89)90854-4. [DOI] [PubMed] [Google Scholar]
  50. Mul Y. M., Rio D. C. Reprogramming the purine nucleotide cofactor requirement of Drosophila P element transposase in vivo. EMBO J. 1997 Jul 16;16(14):4441–4447. doi: 10.1093/emboj/16.14.4441. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. Mullins M. C., Rio D. C., Rubin G. M. cis-acting DNA sequence requirements for P-element transposition. Genes Dev. 1989 May;3(5):729–738. doi: 10.1101/gad.3.5.729. [DOI] [PubMed] [Google Scholar]
  52. Namgoong S. Y., Jayaram M., Kim K., Harshey R. M. DNA-protein cooperativity in the assembly and stabilization of mu strand transfer complex. Relevance of DNA phasing and att site cleavage. J Mol Biol. 1994 May 13;238(4):514–527. doi: 10.1006/jmbi.1994.1311. [DOI] [PubMed] [Google Scholar]
  53. O'Hare K., Rubin G. M. Structures of P transposable elements and their sites of insertion and excision in the Drosophila melanogaster genome. Cell. 1983 Aug;34(1):25–35. doi: 10.1016/0092-8674(83)90133-2. [DOI] [PubMed] [Google Scholar]
  54. Paillard S., Strauss F. Analysis of the mechanism of interaction of simian Ku protein with DNA. Nucleic Acids Res. 1991 Oct 25;19(20):5619–5624. doi: 10.1093/nar/19.20.5619. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. Pyle A. M. Ribozymes: a distinct class of metalloenzymes. Science. 1993 Aug 6;261(5122):709–714. doi: 10.1126/science.7688142. [DOI] [PubMed] [Google Scholar]
  56. Ramsden D. A., McBlane J. F., van Gent D. C., Gellert M. Distinct DNA sequence and structure requirements for the two steps of V(D)J recombination signal cleavage. EMBO J. 1996 Jun 17;15(12):3197–3206. [PMC free article] [PubMed] [Google Scholar]
  57. Rice P., Craigie R., Davies D. R. Retroviral integrases and their cousins. Curr Opin Struct Biol. 1996 Feb;6(1):76–83. doi: 10.1016/s0959-440x(96)80098-4. [DOI] [PubMed] [Google Scholar]
  58. Rice P., Mizuuchi K. Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration. Cell. 1995 Jul 28;82(2):209–220. doi: 10.1016/0092-8674(95)90308-9. [DOI] [PubMed] [Google Scholar]
  59. Rio D. C., Rubin G. M. Identification and purification of a Drosophila protein that binds to the terminal 31-base-pair inverted repeats of the P transposable element. Proc Natl Acad Sci U S A. 1988 Dec;85(23):8929–8933. doi: 10.1073/pnas.85.23.8929. [DOI] [PMC free article] [PubMed] [Google Scholar]
  60. Sarnovsky R. J., May E. W., Craig N. L. The Tn7 transposase is a heteromeric complex in which DNA breakage and joining activities are distributed between different gene products. EMBO J. 1996 Nov 15;15(22):6348–6361. [PMC free article] [PubMed] [Google Scholar]
  61. Savilahti H., Rice P. A., Mizuuchi K. The phage Mu transpososome core: DNA requirements for assembly and function. EMBO J. 1995 Oct 2;14(19):4893–4903. doi: 10.1002/j.1460-2075.1995.tb00170.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  62. Scottoline B. P., Chow S., Ellison V., Brown P. O. Disruption of the terminal base pairs of retroviral DNA during integration. Genes Dev. 1997 Feb 1;11(3):371–382. doi: 10.1101/gad.11.3.371. [DOI] [PubMed] [Google Scholar]
  63. Siebenlist U., Gilbert W. Contacts between Escherichia coli RNA polymerase and an early promoter of phage T7. Proc Natl Acad Sci U S A. 1980 Jan;77(1):122–126. doi: 10.1073/pnas.77.1.122. [DOI] [PMC free article] [PubMed] [Google Scholar]
  64. Staveley B. E., Heslip T. R., Hodgetts R. B., Bell J. B. Protected P-element termini suggest a role for inverted-repeat-binding protein in transposase-induced gap repair in Drosophila melanogaster. Genetics. 1995 Mar;139(3):1321–1329. doi: 10.1093/genetics/139.3.1321. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. Steitz T. A., Steitz J. A. A general two-metal-ion mechanism for catalytic RNA. Proc Natl Acad Sci U S A. 1993 Jul 15;90(14):6498–6502. doi: 10.1073/pnas.90.14.6498. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Taccioli G. E., Gottlieb T. M., Blunt T., Priestley A., Demengeot J., Mizuta R., Lehmann A. R., Alt F. W., Jackson S. P., Jeggo P. A. Ku80: product of the XRCC5 gene and its role in DNA repair and V(D)J recombination. Science. 1994 Sep 2;265(5177):1442–1445. doi: 10.1126/science.8073286. [DOI] [PubMed] [Google Scholar]
  67. Taccioli G. E., Rathbun G., Oltz E., Stamato T., Jeggo P. A., Alt F. W. Impairment of V(D)J recombination in double-strand break repair mutants. Science. 1993 Apr 9;260(5105):207–210. doi: 10.1126/science.8469973. [DOI] [PubMed] [Google Scholar]
  68. Takasu-Ishikawa E., Yoshihara M., Hotta Y. Extra sequences found at P element excision sites in Drosophila melanogaster. Mol Gen Genet. 1992 Mar;232(1):17–23. doi: 10.1007/BF00299132. [DOI] [PubMed] [Google Scholar]
  69. Tuteja N., Tuteja R., Ochem A., Taneja P., Huang N. W., Simoncsits A., Susic S., Rahman K., Marusic L., Chen J. Human DNA helicase II: a novel DNA unwinding enzyme identified as the Ku autoantigen. EMBO J. 1994 Oct 17;13(20):4991–5001. doi: 10.1002/j.1460-2075.1994.tb06826.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  70. Vos J. C., De Baere I., Plasterk R. H. Transposase is the only nematode protein required for in vitro transposition of Tc1. Genes Dev. 1996 Mar 15;10(6):755–761. doi: 10.1101/gad.10.6.755. [DOI] [PubMed] [Google Scholar]
  71. Vos J. C., Plasterk R. H. Tc1 transposase of Caenorhabditis elegans is an endonuclease with a bipartite DNA binding domain. EMBO J. 1994 Dec 15;13(24):6125–6132. doi: 10.1002/j.1460-2075.1994.tb06959.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  72. Weaver D. T. What to do at an end: DNA double-strand-break repair. Trends Genet. 1995 Oct;11(10):388–392. doi: 10.1016/s0168-9525(00)89121-0. [DOI] [PubMed] [Google Scholar]
  73. Werel W., Schickor P., Heumann H. Flexibility of the DNA enhances promoter affinity of Escherichia coli RNA polymerase. EMBO J. 1991 Sep;10(9):2589–2594. doi: 10.1002/j.1460-2075.1991.tb07800.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. Wissmann A., Hillen W. DNA contacts probed by modification protection and interference studies. Methods Enzymol. 1991;208:365–379. doi: 10.1016/0076-6879(91)08020-i. [DOI] [PubMed] [Google Scholar]
  75. Yang J. Y., Jayaram M., Harshey R. M. Positional information within the Mu transposase tetramer: catalytic contributions of individual monomers. Cell. 1996 May 3;85(3):447–455. doi: 10.1016/s0092-8674(00)81122-8. [DOI] [PubMed] [Google Scholar]
  76. Zheng R., Jenkins T. M., Craigie R. Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity. Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13659–13664. doi: 10.1073/pnas.93.24.13659. [DOI] [PMC free article] [PubMed] [Google Scholar]
  77. van Gent D. C., Vink C., Groeneger A. A., Plasterk R. H. Complementation between HIV integrase proteins mutated in different domains. EMBO J. 1993 Aug;12(8):3261–3267. doi: 10.1002/j.1460-2075.1993.tb05995.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  78. van Luenen H. G., Colloms S. D., Plasterk R. H. The mechanism of transposition of Tc3 in C. elegans. Cell. 1994 Oct 21;79(2):293–301. doi: 10.1016/0092-8674(94)90198-8. [DOI] [PubMed] [Google Scholar]

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