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. 1989 Oct 1;263(1):19–23. doi: 10.1042/bj2630019

Secondary structural features of the bacteriophage Mu-encoded A and B transposition proteins.

G Chaconas 1, W D McCubbin 1, C M Kay 1
PMCID: PMC1133385  PMID: 2557821

Abstract

The role of the bacteriophage Mu-encoded A and B proteins is to direct the transposition of Mu DNA. These are the first active DNA transposition proteins to have been purified and their mechanism of action at the biochemical level is under intensive study. Structural studies on these proteins, however, have lagged behind their biochemical characterization. We report here near- and far-u.v. c.d. spectra for these proteins and their secondary structural features derived from these data. The Mu A protein appears to be composed of primarily beta-sheet (40%) with 24% alpha-helix, 9% beta-turn and 27% random coil. In contrast, the Mu B protein contains 55% alpha-helix with only 13% beta-sheet and 3+ beta-turn and 29% random coil. The near-u.v. c.d. spectrum of the A protein was not unusual; however, the profile of the B protein suggested either buried or restricted chromophores within the protein or short-range interactions between aromatic residues.

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Selected References

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

  1. Adzuma K., Mizuuchi K. Target immunity of Mu transposition reflects a differential distribution of Mu B protein. Cell. 1988 Apr 22;53(2):257–266. doi: 10.1016/0092-8674(88)90387-x. [DOI] [PubMed] [Google Scholar]
  2. Bullard B., Mercola D. A., Mommaerts W. F. The origin of the tyrosyl circular dichroism of tropomyosin. Biochim Biophys Acta. 1976 May 20;434(1):90–99. doi: 10.1016/0005-2795(76)90038-6. [DOI] [PubMed] [Google Scholar]
  3. Chaconas G., Giddens E. B., Miller J. L., Gloor G. A truncated form of the bacteriophage Mu B protein promotes conservative integration, but not replicative transposition, of Mu DNA. Cell. 1985 Jul;41(3):857–865. doi: 10.1016/s0092-8674(85)80066-0. [DOI] [PubMed] [Google Scholar]
  4. Chaconas G., Gloor G., Miller J. L. Amplification and purification of the bacteriophage Mu encoded B transposition protein. J Biol Chem. 1985 Mar 10;260(5):2662–2669. [PubMed] [Google Scholar]
  5. Chaconas G., Surette M. G. Mechanism of Mu DNA transposition. Bioessays. 1988 Dec;9(6):205–208. doi: 10.1002/bies.950090606. [DOI] [PubMed] [Google Scholar]
  6. Chou P. Y., Fasman G. D. Prediction of protein conformation. Biochemistry. 1974 Jan 15;13(2):222–245. doi: 10.1021/bi00699a002. [DOI] [PubMed] [Google Scholar]
  7. Craigie R., Arndt-Jovin D. J., Mizuuchi K. A defined system for the DNA strand-transfer reaction at the initiation of bacteriophage Mu transposition: protein and DNA substrate requirements. Proc Natl Acad Sci U S A. 1985 Nov;82(22):7570–7574. doi: 10.1073/pnas.82.22.7570. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Craigie R., Mizuuchi K. Cloning of the A gene of bacteriophage Mu and purification of its product, the Mu transposase. J Biol Chem. 1985 Feb 10;260(3):1832–1835. [PubMed] [Google Scholar]
  9. Craigie R., Mizuuchi K. Mechanism of transposition of bacteriophage Mu: structure of a transposition intermediate. Cell. 1985 Jul;41(3):867–876. doi: 10.1016/s0092-8674(85)80067-2. [DOI] [PubMed] [Google Scholar]
  10. 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]
  11. Craigie R., Mizuuchi M., Mizuuchi K. Site-specific recognition of the bacteriophage Mu ends by the Mu A protein. Cell. 1984 Dec;39(2 Pt 1):387–394. doi: 10.1016/0092-8674(84)90017-5. [DOI] [PubMed] [Google Scholar]
  12. Dufton M. J., Hider R. C. Snake toxin secondary structure predictions. Structure activity relationships. J Mol Biol. 1977 Sep 15;115(2):177–193. doi: 10.1016/0022-2836(77)90095-x. [DOI] [PubMed] [Google Scholar]
  13. Groenen M. A., Timmers E., van de Putte P. DNA sequences at the ends of the genome of bacteriophage Mu essential for transposition. Proc Natl Acad Sci U S A. 1985 Apr;82(7):2087–2091. doi: 10.1073/pnas.82.7.2087. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Groenen M. A., van de Putte P. Analysis of the ends of bacteriophage Mu using site-directed mutagenesis. J Mol Biol. 1986 Jun 20;189(4):597–602. doi: 10.1016/0022-2836(86)90490-0. [DOI] [PubMed] [Google Scholar]
  15. Harshey R. M., Getzoff E. D., Baldwin D. L., Miller J. L., Chaconas G. Primary structure of phage mu transposase: homology to mu repressor. Proc Natl Acad Sci U S A. 1985 Nov;82(22):7676–7680. doi: 10.1073/pnas.82.22.7676. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Janin J. Surface and inside volumes in globular proteins. Nature. 1979 Feb 8;277(5696):491–492. doi: 10.1038/277491a0. [DOI] [PubMed] [Google Scholar]
  17. Maxwell A., Craigie R., Mizuuchi K. B protein of bacteriophage mu is an ATPase that preferentially stimulates intermolecular DNA strand transfer. Proc Natl Acad Sci U S A. 1987 Feb;84(3):699–703. doi: 10.1073/pnas.84.3.699. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. McCubbin W. D., Kay C. M., Narindrasorasak S., Kisilevsky R. Circular-dichroism studies on two murine serum amyloid A proteins. Biochem J. 1988 Dec 15;256(3):775–783. doi: 10.1042/bj2560775. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Miller J. L., Anderson S. K., Fujita D. J., Chaconas G., Baldwin D. L., Harshey R. M. The nucleotide sequence of the B gene of bacteriophage Mu. Nucleic Acids Res. 1984 Nov 26;12(22):8627–8638. doi: 10.1093/nar/12.22.8627. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Miller J. L., Chaconas G. Electron microscopic analysis of in vitro transposition intermediates of bacteriophage Mu DNA. Gene. 1986;48(1):101–108. doi: 10.1016/0378-1119(86)90356-2. [DOI] [PubMed] [Google Scholar]
  21. Mizuuchi K. In vitro transposition of bacteriophage Mu: a biochemical approach to a novel replication reaction. Cell. 1983 Dec;35(3 Pt 2):785–794. doi: 10.1016/0092-8674(83)90111-3. [DOI] [PubMed] [Google Scholar]
  22. Nakayama C., Teplow D. B., Harshey R. M. Structural domains in phage Mu transposase: identification of the site-specific DNA-binding domain. Proc Natl Acad Sci U S A. 1987 Apr;84(7):1809–1813. doi: 10.1073/pnas.84.7.1809. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Pabo C. O., Sauer R. T. Protein-DNA recognition. Annu Rev Biochem. 1984;53:293–321. doi: 10.1146/annurev.bi.53.070184.001453. [DOI] [PubMed] [Google Scholar]
  24. Parker J. M., Guo D., Hodges R. S. New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: correlation of predicted surface residues with antigenicity and X-ray-derived accessible sites. Biochemistry. 1986 Sep 23;25(19):5425–5432. doi: 10.1021/bi00367a013. [DOI] [PubMed] [Google Scholar]
  25. Provencher S. W., Glöckner J. Estimation of globular protein secondary structure from circular dichroism. Biochemistry. 1981 Jan 6;20(1):33–37. doi: 10.1021/bi00504a006. [DOI] [PubMed] [Google Scholar]
  26. Surette M. G., Buch S. J., Chaconas G. Transpososomes: stable protein-DNA complexes involved in the in vitro transposition of bacteriophage Mu DNA. Cell. 1987 Apr 24;49(2):253–262. doi: 10.1016/0092-8674(87)90566-6. [DOI] [PubMed] [Google Scholar]
  27. Teplow D. B., Nakayama C., Leung P. C., Harshey R. M. Structure-function relationships in the transposition protein B of bacteriophage Mu. J Biol Chem. 1988 Aug 5;263(22):10851–10857. [PubMed] [Google Scholar]

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