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

Alison B. Hickman, Hosam E. Ewis, Xianghong Li, Joshua A. Knapp, Thomas Laver, Anna Louise Doss, Gökhan Tolun, Alasdair C. Steven, Alexander Grishaev, Ad Bax, Peter W. Atkinson, Nancy L Craig, Fred Dyda

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)353-367
Number of pages15
JournalCell
Volume158
Issue number2
DOIs
StatePublished - Jul 17 2014

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Transposases
Houseflies
DNA
Dimers
Interspersed Repetitive Sequences
Crystal structure

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Hickman, A. B., Ewis, H. E., Li, X., Knapp, J. A., Laver, T., Doss, A. 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. https://doi.org/10.1016/j.cell.2014.05.037

Structural basis of hAT transposon end recognition by hermes, an octameric dna transposase from musca domestica. / Hickman, Alison B.; Ewis, Hosam E.; Li, Xianghong; Knapp, Joshua A.; Laver, Thomas; Doss, Anna Louise; Tolun, Gökhan; Steven, Alasdair C.; Grishaev, Alexander; Bax, Ad; Atkinson, Peter W.; Craig, Nancy L; Dyda, Fred.

In: Cell, Vol. 158, No. 2, 17.07.2014, p. 353-367.

Research output: Contribution to journalArticle

Hickman, AB, Ewis, HE, Li, X, Knapp, JA, Laver, T, Doss, AL, Tolun, G, Steven, AC, Grishaev, A, Bax, A, Atkinson, PW, Craig, NL & Dyda, F 2014, 'Structural basis of hAT transposon end recognition by hermes, an octameric dna transposase from musca domestica', Cell, vol. 158, no. 2, pp. 353-367. https://doi.org/10.1016/j.cell.2014.05.037
Hickman, Alison B. ; Ewis, Hosam E. ; Li, Xianghong ; Knapp, Joshua A. ; Laver, Thomas ; Doss, Anna Louise ; Tolun, Gökhan ; Steven, Alasdair C. ; Grishaev, Alexander ; Bax, Ad ; Atkinson, Peter W. ; Craig, Nancy L ; Dyda, Fred. / Structural basis of hAT transposon end recognition by hermes, an octameric dna transposase from musca domestica. In: Cell. 2014 ; Vol. 158, No. 2. pp. 353-367.
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