Drosophila IRBP bZIP heterodimer binds P-element DNA and affects hybrid dysgenesis

被引：22

作者：

Francis, Malik Joseph ^{[1
]}

Roche, Siobhan ^{[1
]}

Cho, Michael Jeffrey ^{[1
]}

Beall, Eileen ^{[1
]}

Min, Bosun ^{[1
]}

Panganiban, Ronaldo Paolo ^{[1
]}

Rio, Donald C. ^{[1
,2
,3
]}

机构：

[1] Univ Calif Berkeley, Dept Mol & Cell Biol, 229 Stanley Hall, Berkeley, CA 94720 USA

[2] Univ Calif Berkeley, Ctr RNA Syst Biol, Berkeley, CA 94720 USA

[3] Univ Calif Berkeley, Calif Inst Quantitat Biosci, Berkeley, CA 94720 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2016年 / 113卷 / 46期

关键词：

P-transposable elements; DNA repair; IRBP18/CG6272; Xrp1/CG17836; IRBP complex; STRAND BREAK REPAIR; MOLECULAR-BASIS; TRANSPOSASE; PROTEIN; MELANOGASTER; GENE; EXCISION; IDENTIFICATION; MUTATIONS; STERILITY;

D O I：

10.1073/pnas.1613508113

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 a more general role in maintaining genome stability.

引用

页码：13003 / 13008

页数：6

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