A highly conserved domain of the maize Activator transposase is involved in dimerization

Plant Cell

Volumn 12, Issue 2, 2000, Pages 211-223

  Essers, Lutz ^a,b   Adolphs, Ruth H ^a   Kunze, Reinhard ^a,c  

^a UNIVERSITY OF MUNICH   (Germany)

^b InViTek GmbH   (Germany)

^c UNIVERSITY OF COLOGNE   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

EMBRYOPHYTA; ZEA MAYS;

EID: 0034143320     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.12.2.211     Document Type: Article

References (49)

1. Altschul, S.F., Madden, T.L., Schaffer, A.A., Zhang, J., Zhang, Z., Miller, W., and Lipman, D.J. (1997). Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Res. 25, 3389-3402.
2. Bartel, P., Chien, C.-T., Sternglanz, R., and Fields, S. (1993a). Using the two-hybrid system to detect protein-protein interactions. In Cellular Interactions in Development: A Practical Approach, D.A. Hartley, ed (Oxford: Oxford University Press), pp. 153-179.
3. Bartel, P., Chien, C.-T., Sternglanz, R., and Fields, S. (1993b). Elimination of false positives that arise in using the two-hybrid system. BioTechniques 14, 920-924.
4. Beall, E.L., and Rio, D.C. (1998). Transposase makes critical contacts with, and is stimulated by, single-stranded DNA at the P element termini in vitro. EMBO J. 17, 2122-2136.
5. Becker, H.-A., and Kunze, R. (1997). Maize Activator transposase has a bipartite DNA binding domain that recognizes subterminal motifs and the terminal inverted repeats. Mol. Gen. Genet. 254, 219-230.
6. Behrens-Jung, U., Kühn, S., and Kunze, R. (1994). The Ac transposase consists of several, functionally distinct domains. Maize Genet. Coop. Newsl. 68, 20-21.
7. Boehm, U., Heinlein, M., Behrens, U., and Kunze, R. (1995). One of three nuclear localization signals of maize Activator (Ac) transposase overlaps the DNA-binding domain. Plant J. 7, 441-451.
8. Bolland, S., and Kleckner, N. (1996). The three chemical steps of Tn10/IS10 transposition involve repeated utilization of a single active site. Cell 84, 223-233.
9. Breedon, L., and Nasmyth, K. (1985). Regulation of the yeast HO gene. Cold Spring Harbor Symp. Quant. Biol. 50, 643-650.
10. Chien, C.-T., Bartel, P.L., Sternglanz, R., and Fields, S. (1991). The two-hybrid system: A method to identify and clone genes for proteins that interact with a protein of interest. Proc. Natl. Acad. Sci. USA 88, 9578-9582.
11. Coupland, G., Baker, B., Schell, J., and Starlinger, P. (1988). Characterization of the maize transposable element Ac by internal deletions. EMBO J. 7, 3653-3659.
12. Cuff, J.A., and Barton, G.J. (1999). Evaluation and improvement of multiple sequence methods for protein secondary structure prediction. Proteins 34, 508-519.
13. Cuff, J.A., Clamp, M.E., Siddiqui, A.S., Finlay, M., and Barton, G.J. (1998). JPred: A consensus secondary structure prediction server. Bioinformatics 14, 892-893.
14. Essers, L., and Kunze, R. (1996). A sensitive, quick and semi-quantitative LacZ assay for the two-hybrid system. Trends Genet. 12, 449-450.
15. Feldmar, S., and Kunze, R. (1991). The ORFa protein, the putative transposase of maize transposable element Ac, has a basic DNA binding domain. EMBO J. 10, 4003-4010.
16. Haren, L., Polard, P., Ton Hoang, B., and Chandler, M. (1998). Multiple oligomerization domains in the IS911 transposase: A leucine zipper motif is essential for activity. J. Mol. Biol. 283, 29-41.
17. Hauser, C., Fusswinkel, H., Li, J., Oellig, C., Kunze, R., Müller-Neumann, M., Heinlein, M., Starlinger, P., and Doerfler, W. (1988). Overproduction of the protein encoded by the maize transposable element Ac in insect cells by a baculovirus vector. Mol. Gen. Genet. 214, 373-378.
18. Heinlein, M., Brattig, T., and Kunze, R. (1994). In vivo aggregation of maize Activator (Ac) transposase in nuclei of maize endosperm and petunia protoplasts. Plant J. 5, 705-714.
19. Houba-Hérin, N., Becker, D., Post, A., Larondelle, Y., and Starlinger, P. (1990). Excision of a Ds-like maize transposable element (AcΔ) in a transient assay in petunia is enhanced by a truncated coding region of the transposable element Ac. Mol. Gen. Genet. 224, 17-23.
20. Kämper, J., Reichmann, M., Romeis, T., Bölker, M., and Kahmann, R. (1995). Multiallelic recognition: Nonself-dependent dimerization of the bE and bW homeodomain proteins in Ustilago maydis. Cell 81, 73-83.
21. Kaufman, P.D., and Rio, D.C. (1992). P element transposition in vitro proceeds by a cut-and-paste mechanism and uses GTP as a cofactor. Cell 69, 27-39.
22. Kennedy, A.K., Guhathakurta, A., Kleckner, N., and Haniford, D.B. (1998). Tn10 transposition via a DNA hairpin intermediate. Cell 95, 125-134.
23. Kunze, R. (1996). The Activator (Ac) element of Zea mays L. In Transposable Elements, H. Saedler and A. Gierl, eds (Heidelberg, Germany: Springer-Verlag), pp. 161-194.
24. Kunze, R., and Starlinger, P. (1989). The putative transposase of transposable element Ac from Zea mays L. interacts with subterminal sequences of Ac. EMBO J. 8, 3177-3185.
25. Kunze, R., Stochaj, U., Laufs, J., and Starlinger, P. (1987). Transcription of transposable element Activator (Ac) of Zea mays L. EMBO J. 6, 1555-1563.
26. Kunze, R., Behrens, U., Courage-Franzkowiak, U., Feldmar, S., Kühn, S., and Lütticke, R. (1993). Dominant transposition-deficient mutants of maize Activator (Ac) transposase. Proc. Natl. Acad. Sci. USA 90, 7094-7098.
27. Kunze, R., Fusswinkel, H., and Feldmar, S. (1995a). Expression of plant proteins in baculoviral and bacterial systems. In Methods in Cell Biology-Plant Cell Biology (Part B), D.W. Galbraith, D.P. Bourque, and H.J. Bohnert, eds (Orlando, FL: Academic Press), pp. 461-479.
28. Kunze, R., Kühn, S., Jones, J.D.G., and Scofield, S.R. (1995b). Somatic and germinal activities of maize Activator (Ac) transposase mutants in transgenic tobacco. Plant J. 8, 45-54.
29. Lavoie, B.D., Chan, B.S., Allison, R.G., and Chaconas, G. (1991). Structural aspects of a higher order nucleoprotein complex: Induction of an altered DNA structure at the Mu-host junction of the Mu type 1 transpososome. EMBO J. 10, 3051-3059.
30. Li, M.-G., and Starlinger, P. (1990). Mutational analysis of the N terminus of the protein of maize transposable element Ac. Proc. Natl. Acad. Sci. USA 87, 6044-6048.
31. Lohe, A.R., Sullivan, D.T., and Hartl, D.L. (1996). Subunit interactions in the mariner transposase. Genetics 144, 1087-1095.
32. Mahnke Braam, L.A., and Reznikoff, W.S. (1998). Functional characterization of the Tn5 transposase by limited proteolysis. J. Biol. Chem. 273, 10908-10913.
33. Mahnke Braam, L.A., Goryshin, I.V., and Reznikoff, W.S. (1999). A mechanism for Tn5 inhibition: Carboxyl-terminal dimerization. J. Biol. Chem. 274, 86-92.
34. McClintock, B. (1951). Chromosome organization and genic expression. Cold Spring Harbor Symp. Quant. Biol. 16, 13-47.
35. Miller, J.H. (1972). Experiments in Molecular Genetics. (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press).
36. Mizuuchi, M., Baker, T.A., and Mizuuchi, K. (1995). Assembly of phage Mu transpososomes: Cooperative transitions assisted by protein and DNA scaffolds. Cell 83, 375-385.
37. Raina, R., Schlappi, M., Karunanandaa, B., Elhofy, A., and Fedororf, N. (1998). Concerted formation of macromolecular Suppressormutator transposition complexes. Proc. Natl. Acad. Sci. USA 95, 8526-8531.
38. Sarnovsky, R.J., May, E.W., and Craig, N.L. (1996). The Tn7 transposase is a heteromeric compleix in which DNA breakage and joining activities are distributed between different gene products. EMBO J. 15, 6348-6361.
39. Sato, T., Hanada, M., Bodrug, S., Irie, S.J., Iwama, N., Boise, L.H., Thompson, C.B., Golemis, E., Fong, L., Wang, H.G., and Reed, J.C. (1994). Interactions among members of the Bcl-2 protein family analyzed with a yeast two-hybrid system. Proc. Natl. Acad. Sci. USA 91, 9238-9242.
40. Scofield, S.R., English, J.J., and Jones, J.D.G. (1993). High level expression of the Activator (Ac) transposase gene inhibits the excision of Dissociation (Ds) in tobacco cotyledons. Cell 75, 507-517.
41. Stellwagen, A.E., and Craig, N.L. (1997). Avoiding self - Two Tn7-encoded proteins mediate target immunity in Tn7 transposition. EMBO J. 16, 6823-6834.
42. Stellwagen, A.E., and Craig, N.L. (1998). Mobile DNA elements: Controlling transposition with ATP-dependent molecular switches. Trends Biochem. Sci. 23, 486-490.
43. Studier, F.W., Rosenberg, A.H., Dunn, J.J., and Dubendorff, J.W. (1990). Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185, 60-89.
44. Trentmann, S.M., Saedler, H., and Gierl, A. (1993). The transposable element En/Spm-encoded TNPA protein contains a DNA binding and a dimerization domain. Mol. Gen. Genet. 238, 201-208.
45. van Pouderoyen, G., Ketting, R.F., Perrakis, A., Plasterk, R.H., and Sixma, T.K. (1997). Crystal structure of the specific DNA-binding domain of Tc3 transposase of C. elegans in complex with transposon DNA. EMBO J. 16, 6044-6054.
46. Vos, J.C., De Baere, I., and Plasterk, R.H.A. (1996). Transposase is the only nematode protein required for in vitro transposition of Tc1. Genes Dev. 10, 755-761.
47. Weinreich, M.D., Gasch, A., and Reznikoff, W.S. (1994). Evidence that the cis preference of the Tn5 transposase is caused by nonproductive multimerization. Genes Dev. 8, 2363-2374.
48. Wu, Z.G., and Chaconas, G. (1995). A novel DNA binding and nuclease activity in domain III of Mu transposase: Evidence for a catalytic region involved in donor cleavage. EMBO J. 14, 3835-3843.
49. Zhang, Z., Schaffer, A.A., Miller, W., Madden, T.L., Lipman, D.J., Koonin, E.V., and Altschul, S.F. (1998). Protein sequence similarity searches using patterns as seeds. Nucleic Acids Res. 26, 3986-3990.