Proteomics

Dataset Information

0

Identification of phosphorylation sites in piggyBac transposase N-terminus


ABSTRACT: The piggyBac transposon system is widely used for biotechnology and genome engineering and is the founding member of a large superfamily of piggyBac-like elements. We investigated the role in transpositon of the nonconserved N-terminus in the piggyBac transposase, including the impact of predicted casein kinase phosphorylation sites within it.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell

SUBMITTER: Alison Hickman  

LAB HEAD: Fred Dyda

PROVIDER: PXD037132 | Pride | 2023-03-11

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
77180_93453.mzid.gz Mzid
77180_93453.pep.xml Pepxml
93453.mzXML Mzxml
93453.raw Raw
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Publications

Transposase N-terminal phosphorylation and asymmetric transposon ends inhibit piggyBac transposition in mammalian cells.

Luo Wentian W   Hickman Alison B AB   Genzor Pavol P   Ghirlando Rodolfo R   Furman Christopher M CM   Menshikh Anna A   Haase Astrid A   Dyda Fred F   Wilson Matthew H MH  

Nucleic acids research 20221201 22


DNA transposon systems are widely used in mammalian cells for genetic modification experiments, but their regulation remains poorly understood. We used biochemical and cell-based assays together with AlphaFold modeling and rational protein redesign to evaluate aspects of piggyBac transposition including the previously unexplained role of the transposase N-terminus and the need for asymmetric transposon ends for cellular activity. We found that phosphorylation at predicted casein kinase II sites  ...[more]

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