Dimerization through the RING-Finger Domain Attenuates Excision Activity of the piggyBac Transposase

Sharma, Rahul and Nirwal, Shivlee and Narayanan, Naveen (2018) Dimerization through the RING-Finger Domain Attenuates Excision Activity of the piggyBac Transposase. Biochemistry, 57. pp. 2913-2922.

[img] PDF
acs.biochem.7b01191.pdf - Published Version
Restricted to Registered users only

Download (3MB) | Request a copy

Abstract

The movement of the piggyBac transposon is mediated through its cognate transposase. The piggyBac transposase binds to the terminal repeats present at the ends of the transposon. This is followed by excision of the transposon and release of the nucleoprotein complex. The complex translocates, followed by integration of the transposon at the target site. Here, we show that the RING-finger domain (RFD) present toward the C-terminus of the transposase is vital for dimerization of this enzyme. The deletion of the RFD or the last seven residues of the RFD results in a monomeric protein that binds the terminal end of the transposon with nearly the same affinity as wild type piggyBac transposase. Surprisingly, the monomeric constructs exhibit >2-fold enhancement in the excision activity of the enzyme. Overall, our studies suggest that dimerization attenuates the excision activity of the piggyBac transposase. This attribute of the piggyBac transposase may serve to prevent excessive transposition of the piggyBac transposon that might be catastrophic for the host cell.

Item Type: Article
Subjects: Research > Research Center - Health Sciences
Depositing User: KMC Library
Date Deposited: 14 Feb 2019 03:55
Last Modified: 14 Feb 2019 03:55
URI: http://eprints.manipal.edu/id/eprint/153274

Actions (login required)

View Item View Item