<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Helou L</submitter><funding>Ligue Contre le Cancer</funding><funding>Conseil Régional du Centre-Val de Loire</funding><funding>Division of Cancer Prevention, National Cancer Institute</funding><funding>NCI NIH HHS</funding><funding>Société Nationale Française de Gastro-Entérologie</funding><pagination>166805</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8426422</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>433(7)</volume><pubmed_abstract>PiggyBac(PB)-like elements (pble) are members of a eukaryotic DNA transposon family. This family is of interest to evolutionary genomics because pble transposases have been domesticated at least 9 times in vertebrates. The amino acid sequence of pble transposases can be split into three regions: an acidic N-terminal domain (~100 aa), a central domain (~400 aa) containing a DD[D/E] catalytic triad, and a cysteine-rich domain (CRD; ~90 aa). Two recent reports suggested that a functional CRD is required for pble transposase activity. Here we found that two CRD-deficient pble transposases, a PB variant and an isoform encoded by the domesticated PB-derived vertebrate transposase gene 5 (pgbd5) trigger transposition of the Ifp2 pble. When overexpressed in HeLa cells, these CRD-deficient transpos</pubmed_abstract><journal>Journal of molecular biology</journal><pubmed_title>The C-terminal Domain of piggyBac Transposase Is Not Required for DNA Transposition.</pubmed_title><pmcid>PMC8426422</pmcid><funding_grant_id>P30 CA008748</funding_grant_id><funding_grant_id>R01 CA214812</funding_grant_id><pubmed_authors>Helou L</pubmed_authors><pubmed_authors>Dardente H</pubmed_authors><pubmed_authors>Guillou F</pubmed_authors><pubmed_authors>Beauclair L</pubmed_authors><pubmed_authors>Buisine N</pubmed_authors><pubmed_authors>Kentsis A</pubmed_authors><pubmed_authors>Jaszczyszyn Y</pubmed_authors><pubmed_authors>Arensburger P</pubmed_authors><pubmed_authors>Bigot Y</pubmed_authors><pubmed_authors>Lecomte T</pubmed_authors></additional><is_claimable>false</is_claimable><name>The C-terminal Domain of piggyBac Transposase Is Not Required for DNA Transposition.</name><description>PiggyBac(PB)-like elements (pble) are members of a eukaryotic DNA transposon family. This family is of interest to evolutionary genomics because pble transposases have been domesticated at least 9 times in vertebrates. The amino acid sequence of pble transposases can be split into three regions: an acidic N-terminal domain (~100 aa), a central domain (~400 aa) containing a DD[D/E] catalytic triad, and a cysteine-rich domain (CRD; ~90 aa). Two recent reports suggested that a functional CRD is required for pble transposase activity. Here we found that two CRD-deficient pble transposases, a PB variant and an isoform encoded by the domesticated PB-derived vertebrate transposase gene 5 (pgbd5) trigger transposition of the Ifp2 pble. When overexpressed in HeLa cells, these CRD-deficient transpos</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Apr</publication><modification>2026-05-09T03:10:58.138Z</modification><creation>2025-02-18T23:36:40.797Z</creation></dates><accession>S-EPMC8426422</accession><cross_references><pubmed>33450253</pubmed><doi>10.1016/j.jmb.2020.166805</doi></cross_references></HashMap>