Literature summary for 2.7.7.B22 extracted from

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

Search for more literature for 2.7.7.B22

Cloned(Commentary)

Cloned (Comment)	Organism
full-length Hermes expressed in eukaryotic cells, such as budding yeast and Sf9 cells, similarly forms a large multimeric species consistent with an octamer as judged by gel filtration	Musca domestica

Protein Variants

Protein Variants	Comment	Organism
additional information	introduction of three point mutations into the interface disrupting the octamer shows that the resulting dimers are catalytically active in vitro. Generation of dimers by deleting the helix and surrounding residues, HermesDELTA497-516, also leads to active dimers in vitro, that can catalyze all of the catalytic steps. Although Hermes dimers are hyperactive in vitro at low ionic strength, their activities are severely reduced under more physiologically relevant conditions. Hermes dimers are inactive in vivo	Musca domestica

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Musca domestica	formation of a Hermes transposase-DNA complex. Bipartite DNA recognition at hAT transposon ends and Hermes-DNA interactions within the transpososome. No protein-DNA interactions involving bp 12-16 of the TIR. The avidity provided by multiple sites of interaction allows a transposase to locate its transposon ends amidst a sea of chromosomal DNA, mechanism, overview. The enzyme possesses a RNaseH-like catalytic domain interrupted by a large [.alpha]-helical insertion domain, and an N-terminal intertwined dimerization domain. Together, these domains catalyze the chemical steps of DNA nicking, hairpin formation, and DNA strand transfer that comprise hAT transposition	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Musca domestica	Q25442	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	formation of a Hermes transposase-DNA complex. Bipartite DNA recognition at hAT transposon ends and Hermes-DNA interactions within the transpososome. No protein-DNA interactions involving bp 12-16 of the TIR. The avidity provided by multiple sites of interaction allows a transposase to locate its transposon ends amidst a sea of chromosomal DNA, mechanism, overview. The enzyme possesses a RNaseH-like catalytic domain interrupted by a large [.alpha]-helical insertion domain, and an N-terminal intertwined dimerization domain. Together, these domains catalyze the chemical steps of DNA nicking, hairpin formation, and DNA strand transfer that comprise hAT transposition	Musca domestica	?	-	?

Subunits

Subunits	Comment	Organism
More	while 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 non-specific DNA binding surfaces for target capture, bipartite DNA recognition at hAT transposon ends. Overall architecture of the Hermes transpososome, the nucleoprotein assembly that carries out DNA transposition, overview	Musca domestica
octamer	a tetramer of dimers, the dimer is the fundamental catalytic unit	Musca domestica

Synonyms

Synonyms	Comment	Organism
DNA transposase	-	Musca domestica
Hermes	-	Musca domestica

General Information

General Information	Comment	Organism
evolution	enzyme Hermes is a member of the hAT transposon superfamily, which has active representatives, including McClintock's archetypal Ac mobile genetic element, in many eukaryotic species	Musca domestica

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Release 2023.1 (January 2023)