Structural basis of hAT transposon end recognition by Hermes, an octameric DNA transposase from Musca domestica.

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TitleStructural basis of hAT transposon end recognition by Hermes, an octameric DNA transposase from Musca domestica.
Publication TypeJournal Article
Year of Publication2014
AuthorsHickman, AB, Ewis, HE, Li, X, Knapp, JA, Laver, T, Doss, A-L, Tolun, G, Steven, AC, Grishaev, A, Bax, A, Atkinson, PW, Craig, NL, Dyda, F
JournalCell
Volume158
Issue2
Pagination353-67
Date Published2014 Jul 17
ISSN1097-4172
KeywordsAnimals, Base Sequence, Crystallography, X-Ray, Dimerization, DNA Transposable Elements, Houseflies, Insect Proteins, Models, Molecular, Molecular Sequence Data, RNA-Binding Proteins, Transposases
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.

DOI10.1016/j.cell.2014.05.037
Alternate JournalCell
PubMed ID25036632
PubMed Central IDPMC4105704
Grant ListZ01 DK036153-01 / / Intramural NIH HHS / United States