Mariner Mos1 Transposase Dimerizes Prior to ITR Binding

Augé-Gouillou, Corinne; Brillet, Benjamin; Germon, Stéphanie; Hamelin, Marie‐Hélène; Bigot, Yves

doi:10.1016/j.jmb.2005.05.019

Cited by 42 publications

(61 citation statements)

References 34 publications

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“…3b and data not shown). The location of the MAR-binding site within the Hsmar1 TIR is consistent with those of other mariner transposase-binding sites (26,31).…”

Section: Resultssupporting

confidence: 78%

Birth of a chimeric primate gene by capture of the transposase gene from a mobile element

Cordaux

Udit

Batzer

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

226

264

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The emergence of new genes and functions is of central importance to the evolution of species. The contribution of various types of duplications to genetic innovation has been extensively investigated. Less understood is the creation of new genes by recycling of coding material from selfish mobile genetic elements. To investigate this process, we reconstructed the evolutionary history of SETMAR, a new primate chimeric gene resulting from fusion of a SET histone methyltransferase gene to the transposase gene of a mobile element. We show that the transposase gene was recruited as part of SETMAR 40 -58 million years ago, after the insertion of an Hsmar1 transposon downstream of a preexisting SET gene, followed by the de novo exonization of previously noncoding sequence and the creation of a new intron. The original structure of the fusion gene is conserved in all anthropoid lineages, but only the N-terminal half of the transposase is evolving under strong purifying selection. In vitro assays show that this region contains a DNA-binding domain that has preserved its ancestral binding specificity for a 19-bp motif located within the terminal-inverted repeats of Hsmar1 transposons and their derivatives. The presence of these transposons in the human genome constitutes a potential reservoir of Ϸ1,500 perfect or nearly perfect SETMAR-binding sites. Our results not only provide insight into the conditions required for a successful gene fusion, but they also suggest a mechanism by which the circuitry underlying complex regulatory networks may be rapidly established.transposable elements ͉ gene fusion ͉ molecular domestication ͉ DNA binding ͉ regulatory network

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“…3b and data not shown). The location of the MAR-binding site within the Hsmar1 TIR is consistent with those of other mariner transposase-binding sites (26,31).…”

Section: Resultssupporting

confidence: 78%

Birth of a chimeric primate gene by capture of the transposase gene from a mobile element

Cordaux

Udit

Batzer

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

226

264

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“…Logically, we asked where the DNA-binding activity of FHY3 and FAR1 derived from. Notably, all eukary- otic transposases that have been biochemically characterized so far possess two functionally separable domains: an N-terminal region that binds to the terminal inverted repeats of the cognate transposons and a central or C-terminal region that catalyzes the cleavage and transfer reactions of the cut-and-paste transposition reaction (Haren et al, 1999;Lisch, 2002;Michel et al, 2003;Augé-Gouillou et al, 2005;Feschotte et al, 2005). FHY3 and FAR1 share an N-terminal C2H2 zinc finger domain of the WRKY-GCM1 family with MULE transposases (Babu et al, 2006;Lin et al, 2007).…”

Section: Discrete and Essential Roles Of The Multiple Domains Of Fhy3mentioning

confidence: 99%

Discrete and Essential Roles of the Multiple Domains of Arabidopsis FHY3 in Mediating Phytochrome A Signal Transduction

et al. 2008

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Phytochrome A is the primary photoreceptor for mediating various far-red light-induced responses in higher plants. We recently showed that Arabidopsis (Arabidopsis thaliana) FAR-RED ELONGATED HYPOCOTYL3 (FHY3) and FAR-RED-IMPAIRED RESPONSE1 (FAR1), a pair of homologous proteins sharing significant sequence homology to Mutator-like transposases, act as novel transcription factors essential for activating the expression of FHY1 and FHL (for FHY1-like), whose products are required for light-induced phytochrome A nuclear accumulation and subsequent light responses. FHY3, FAR1, and Mutator-like transposases also share a similar domain structure, including an N-terminal C2H2 zinc finger domain, a central putative core transposase domain, and a C-terminal SWIM motif (named after SWI2/SNF and MuDR transposases). In this study, we performed a promoter-swapping analysis of FHY3 and FAR1. Our results suggest that the partially overlapping functions of FHY3 and FAR1 entail divergence of their promoter activities and protein subfunctionalization. To gain a better understanding of the molecular mode of FHY3 function, we performed a structure-function analysis, using site-directed mutagenesis and transgenic approaches. We show that the conserved N-terminal C2H2 zinc finger domain is essential for direct DNA binding and biological function of FHY3 in mediating light signaling, whereas the central core transposase domain and C-terminal SWIM domain are essential for the transcriptional regulatory activity of FHY3 and its homodimerization or heterodimerization with FAR1. Furthermore, the ability to form homodimers or heterodimers largely correlates with the transcriptional regulatory activity of FHY3 in plant cells. Together, our results reveal discrete roles of the multiple domains of FHY3 and provide functional support for the proposition that FHY3 and FAR1 represent transcription factors derived from a Mutator-like transposase(s).

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“…For Mu transposase, DNA binding actually promotes tetramer formation (17)(18)(19). In V(D)J recombination, a dimeric complex of RAG2 and a dimer or trimer of RAG1 protein recognizes the recombination signal sequence (20,21); for the Hermes transposase a hexamer is the active species (16); for the mariner family transposase, Mos1 is a dimer or tetramer (22)(23)(24)(25); and for the mariner family member, Himar 1, is a tetramer (26). For Tn5 and Tn10, the protein acts as a dimer, with a single active site acting in trans at each transposon end (27)(28)(29)(30).…”

mentioning

confidence: 99%

Analysis of P Element Transposase Protein-DNA Interactions during the Early Stages of Transposition

Tang

Cecconi

Bustamante

et al. 2007

Journal of Biological Chemistry

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P elements are a family of transposable elements found inDrosophila that move by using a cut-and-paste mechanism and that encode a transposase protein that uses GTP as a cofactor for transposition. Here we used atomic force microscopy to visualize the initial interaction of transposase protein with P element DNA. The transposase first binds to one of the two P element ends, in the presence or absence of GTP, prior to synapsis. In the absence of GTP, these complexes remain stable but do not proceed to synapsis. In the presence of GTP or nonhydrolyzable GTP analogs, synapsis happens rapidly, whereas DNA cleavage is slow. Both atomic force microscopy and standard biochemical methods have been used to show that the P element transposase exists as a pre-formed tetramer that initially binds to either one of the two P element ends in the absence of GTP prior to synapsis. This initial single end binding may explain some of the aberrant P element-induced rearrangements observed in vivo, such as hybrid end insertion. The allosteric effect of GTP in promoting synapsis by P element transposase may be to orient a second site-specific DNA binding domain in the tetramer allowing recognition of a second high affinity transposase-binding site at the other transposon end.Mobile genetic elements are ubiquitous among both prokaryotic and eukaryotic organisms (1). Genome sequencing projects have shown that transposable elements make up a substantial fraction of eukaryotic genomes, including 49% of the human genome (2, 3). These mobile elements can lead to mutations and genome rearrangements and appear to play a role in genome evolution (4, 5). The mechanisms by which transposons are mobilized can be grouped based upon whether there is a DNA or an RNA intermediate (1,4,5). P elements use a cut-and-paste mechanism with a DNA intermediate, related to those used by the Tn5, Tn10, and Tn7 prokaryotic transposons and the eukaryotic Tc1/mariner family (6 -8). Studies of P element transposition in vitro have demonstrated cofactor requirements for both GTP and magnesium ions (Mg 2ϩ ) (6, 9 -11). Although divalent metal ions are universally required cofactors for transposase proteins (1, 12, 13), the P element reaction is unique among this family of polynucleotidyltransferases in the use of GTP as a cofactor (9). Recent studies have shown that GTP promotes pre-cleavage synaptic complex assembly between the P element termini and the transposase protein (14). Previous in vitro studies had also shown that nonhydrolyzable GTP analogs support both the P element DNA cleavage and joining reactions (9). Furthermore, GTP does not effect the binding of P element transposase to the high affinity sites near the transposon termini, as assayed by DNase I footprinting (9, 15). Whereas some transposon systems have been studied with respect to the assembly state of their transposase, the oligomeric state of the active P element transposase protein and how it initially interacts with P element DNA are unknown. In cases where it has been studied, other transpos...

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Mariner Mos1 Transposase Dimerizes Prior to ITR Binding

Cited by 42 publications

References 34 publications

Birth of a chimeric primate gene by capture of the transposase gene from a mobile element

Birth of a chimeric primate gene by capture of the transposase gene from a mobile element

Discrete and Essential Roles of the Multiple Domains of Arabidopsis FHY3 in Mediating Phytochrome A Signal Transduction

Analysis of P Element Transposase Protein-DNA Interactions during the Early Stages of Transposition

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