TY - JOUR
T1 - Drosophila IRBP bZIP heterodimer binds P-element DNA and affects hybrid dysgenesis
AU - Francis, Malik Joseph
AU - Roche, Siobhan
AU - Cho, Michael Jeffrey
AU - Beall, Eileen
AU - Min, Bosun
AU - Panganiban, Ronaldo Paolo
AU - Rio, Donald C.
PY - 2016/11/15
Y1 - 2016/11/15
N2 - In Drosophila, P-element transposition causes mutagenesis and genome instability during hybrid dysgenesis. The P-element 31-bp terminal inverted repeats (TIRs) contain sequences essential for transposase cleavage and have been implicated in DNA repair via protein-DNA interactions with cellular proteins. The identity and function of these cellular proteins were unknown. Biochemical characterization of proteins that bind the TIRs identified a heterodimeric basic leucine zipper (bZIP) complex between an uncharacterized protein that we termed "Inverted Repeat Binding Protein (IRBP) 18" and its partner Xrp1. The reconstituted IRBP18/Xrp1 heterodimer binds sequence-specifically to its dsDNA-binding site within the P-element TIRs. Genetic analyses implicate both proteins as critical for repair of DNA breaks following transposase cleavage in vivo. These results identify a cellular protein complex that binds an active mobile element and plays amore general role in maintaining genome stability.
AB - In Drosophila, P-element transposition causes mutagenesis and genome instability during hybrid dysgenesis. The P-element 31-bp terminal inverted repeats (TIRs) contain sequences essential for transposase cleavage and have been implicated in DNA repair via protein-DNA interactions with cellular proteins. The identity and function of these cellular proteins were unknown. Biochemical characterization of proteins that bind the TIRs identified a heterodimeric basic leucine zipper (bZIP) complex between an uncharacterized protein that we termed "Inverted Repeat Binding Protein (IRBP) 18" and its partner Xrp1. The reconstituted IRBP18/Xrp1 heterodimer binds sequence-specifically to its dsDNA-binding site within the P-element TIRs. Genetic analyses implicate both proteins as critical for repair of DNA breaks following transposase cleavage in vivo. These results identify a cellular protein complex that binds an active mobile element and plays amore general role in maintaining genome stability.
UR - https://www.scopus.com/pages/publications/84995580499
UR - https://www.scopus.com/pages/publications/84995580499#tab=citedBy
U2 - 10.1073/pnas.1613508113
DO - 10.1073/pnas.1613508113
M3 - Article
C2 - 27799520
AN - SCOPUS:84995580499
SN - 0027-8424
VL - 113
SP - 13003
EP - 13008
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 46
ER -