Literature summary for 2.7.7.B22 extracted from

Sharma, R.; Nirwal, S.; Narayanan, N.; Nair, D.T.
Dimerization through the RING-finger domain attenuates excision activity of the piggyBac transposase (2018), Biochemistry, 57, 2913-2922 .

Search for more literature for 2.7.7.B22

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	the RING-finger domain binds two Zn2+ ions through the C2C2CHC2 motif. A mutant lacking the RING-finger domain does not show the presence of Zn2+ ions	Trichoplusia ni

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
86000	-	gel filtration, mutant lacking the RING-finger domain	Trichoplusia ni
121000	-	gel filtration, wild-type	Trichoplusia ni

Organism

Organism	UniProt	Comment	Textmining
Trichoplusia ni	Q27026	-	-

Subunits

Subunits	Comment	Organism
dimer	2 * 68000, wild-type, calulated from sequence	Trichoplusia ni
monomer	1 * 64000, mutant lacking the RING-finger domain, calculated from sequence	Trichoplusia ni
More	the C-terminal 7 residues of the RING-finger domain are critical for dimer formation	Trichoplusia ni

Synonyms

Synonyms	Comment	Organism
DDE_Tnp_1_7 domain-containing protein	-	Trichoplusia ni
piggyBac transposase	-	Trichoplusia ni

General Information

General Information	Comment	Organism
physiological function	the RING-finger domain present toward the C-terminus of the transposase is vital for dimerization of this enzyme. The deletion of the RING-finger domain or the last seven residues of the RING-finger domain results in a monomeric protein that binds the terminal end of the transposon with nearly the same affinity as wild type piggyBac transposase. The monomeric constructs exhibit more than 2fold enhancement in the excision activity of the enzyme	Trichoplusia ni

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)