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Structural basis of hAT transposon end recognition by hermes, an octameric dna transposase from musca domestica

Journal Article


Abstract


  • Hermes is a member of the hAT transposon superfamily that has active representatives, including McClintock's archetypal Ac mobile genetic element, in many eukaryotic species. The crystal structure of the Hermes transposase-DNA complex reveals that Hermes forms an octameric ring organized as a tetramer of dimers. Although isolated dimers are active in vitro for all the chemical steps of transposition, only octamers are active in vivo. The octamer can provide not only multiple specific DNA-binding domains to recognize repeated subterminal sequences within the transposon ends, which are important for activity, but also multiple nonspecific DNA binding surfaces for target capture. The unusual assembly explains the basis of bipartite DNA recognition at hAT transposon ends, provides a rationale for transposon end asymmetry, and suggests how the avidity provided by multiple sites of interaction could allow a transposase to locate its transposon ends amidst a sea of chromosomal DNA.

UOW Authors


  •   Hickman, Alison (external author)
  •   Ewis, Hosam (external author)
  •   Li, Xianghong (external author)
  •   Knapp, Joshua (external author)
  •   Laver, Thomas (external author)
  •   Doss, Anna-Louise (external author)
  •   Tolun, Gokhan
  •   Steven, Alasdair (external author)
  •   Grishaev, Alexander (external author)
  •   Bax, Ad (external author)
  •   Atkinson, Peter (external author)
  •   Craig, Nancy (external author)
  •   Dyda, Fred (external author)

Publication Date


  • 2014

Published In


Citation


  • Hickman, A. B., Ewis, H. E., Li, X., Knapp, J. A., Laver, T., Doss, A., Tolun, G., Steven, A. C., Grishaev, A., Bax, A., Atkinson, P. W., Craig, N. L. & Dyda, F. (2014). Structural basis of hAT transposon end recognition by hermes, an octameric dna transposase from musca domestica. Cell, 158 (2), 353-367.

Scopus Eid


  • 2-s2.0-84904538844

Number Of Pages


  • 14

Start Page


  • 353

End Page


  • 367

Volume


  • 158

Issue


  • 2

Place Of Publication


  • United States

Abstract


  • Hermes is a member of the hAT transposon superfamily that has active representatives, including McClintock's archetypal Ac mobile genetic element, in many eukaryotic species. The crystal structure of the Hermes transposase-DNA complex reveals that Hermes forms an octameric ring organized as a tetramer of dimers. Although isolated dimers are active in vitro for all the chemical steps of transposition, only octamers are active in vivo. The octamer can provide not only multiple specific DNA-binding domains to recognize repeated subterminal sequences within the transposon ends, which are important for activity, but also multiple nonspecific DNA binding surfaces for target capture. The unusual assembly explains the basis of bipartite DNA recognition at hAT transposon ends, provides a rationale for transposon end asymmetry, and suggests how the avidity provided by multiple sites of interaction could allow a transposase to locate its transposon ends amidst a sea of chromosomal DNA.

UOW Authors


  •   Hickman, Alison (external author)
  •   Ewis, Hosam (external author)
  •   Li, Xianghong (external author)
  •   Knapp, Joshua (external author)
  •   Laver, Thomas (external author)
  •   Doss, Anna-Louise (external author)
  •   Tolun, Gokhan
  •   Steven, Alasdair (external author)
  •   Grishaev, Alexander (external author)
  •   Bax, Ad (external author)
  •   Atkinson, Peter (external author)
  •   Craig, Nancy (external author)
  •   Dyda, Fred (external author)

Publication Date


  • 2014

Published In


Citation


  • Hickman, A. B., Ewis, H. E., Li, X., Knapp, J. A., Laver, T., Doss, A., Tolun, G., Steven, A. C., Grishaev, A., Bax, A., Atkinson, P. W., Craig, N. L. & Dyda, F. (2014). Structural basis of hAT transposon end recognition by hermes, an octameric dna transposase from musca domestica. Cell, 158 (2), 353-367.

Scopus Eid


  • 2-s2.0-84904538844

Number Of Pages


  • 14

Start Page


  • 353

End Page


  • 367

Volume


  • 158

Issue


  • 2

Place Of Publication


  • United States