Transposable elements controlling I-R hybrid dysgenesis in D. melanogaster are similar to mammalian LINEs

Fawcett, Diana; Lister, Clare; Kellett, Elaine; Finnegan, David J.

doi:10.1016/0092-8674(86)90815-9

Cited by 238 publications

(171 citation statements)

References 54 publications

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“…The 3′ end of the NCR is characterized by the presence of a variable tandem repeats (TCAA n or CAA n ). These features are different from the fruit fly (Fawcett et al, 1986) or mosquito (Tu and Hill, 1999) I elements that have either poly (A) or "TAA" tandem repeats. These nimbus (BgI) variable tandem repeats are AT rich (75%), and define the junction of the 3′ target site duplication (TSD) at the end of each element in cis.…”

Section: Identification and Sequence Analysis Of Nimbus (Bgi) A Novementioning

confidence: 99%

Nimbus (BgI): An active non-LTR retrotransposon of the Schistosoma mansoni snail host Biomphalaria glabrata

Raghavan

Tettelin²,

Miller

et al. 2007

International Journal for Parasitology

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The freshwater snail Biomphalaria glabrata is closely associated with the transmission of human schistosomiasis. An ecologically sound method has been proposed to control schistosomiasis using genetically modified snails to displace endemic, susceptible ones. To assess the viability of this form of biological control, studies towards understanding the molecular makeup of the snail relative to the presence of endogenous mobile genetic elements are being undertaken since they can be exploited for genetic transformation studies. We previously cloned a 1.95 Kb BamHI fragment in B. glabrata (BGR2) with sequence similarity to the human long interspersed nuclear element (LINE or L1). A contiguous, full-length sequence corresponding to BGR2, hereafter-named nimbus (BgI), has been identified from a B. glabrata bacterial artificial chromosome (BAC) library. Sequence analysis of the 65,764 bp BAC insert contained one full-length, complete nimbus (BgI) element (element I), two full-length elements (elements II and III) containing deletions and flanked by target site duplications and 10 truncated copies. The intact nimbus (BgI) contained two open reading frames (ORFs 1 and 2) encoding the characteristic hallmark domains found in non-long terminal repeat retrotransposons belonging to the I clade; a nucleic acid binding protein in ORF1 and an apurinic/ apyrimidinic endonuclease, reverse transcriptase and RNase H in ORF2. Phylogenetic analysis revealed that nimbus (BgI) is closely related to Drosophila (I factor), mosquito Aedes aegypti (MosquI) and chordate ascidian Ciona intestinalis (CiI) retrotransposons. Nimbus (BgI) represents the first complete mobile element characterized from a mollusk that appears to be transcriptionally active and is widely distributed in snails of the neotropics and the Old World.

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Section: Identification and Sequence Analysis Of Nimbus (Bgi) A Novementioning

confidence: 99%

Nimbus (BgI): An active non-LTR retrotransposon of the Schistosoma mansoni snail host Biomphalaria glabrata

Raghavan

Tettelin²,

Miller

et al. 2007

International Journal for Parasitology

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“…RNH domains have also been found in several lineages of non-LTR retrotransposons (Fawcett et al 1986;Doolittle et al 1989;Blesa and Martinez-Sebastian 1997). One early study proposed the presence of RNH domains in a wider range of non-LTR element lineages (McClure 1991).…”

mentioning

confidence: 98%

Phylogenetic Analysis of Ribonuclease H Domains Suggests a Late, Chimeric Origin of LTR Retrotransposable Elements and Retroviruses

Malik¹,

Eickbush²

2001

Genome Res.

217

200

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We have conducted a phylogenetic analysis of the Ribonuclease HI (RNH) domains present in Eubacteria, Eukarya, all long-term repeat (LTR)-bearing retrotransposons, and several late-branching clades of non-LTR retrotransposons. Analysis of this simple yet highly conserved enzymatic domain from these disparate sources provides surprising insights into the evolution of eukaryotic retrotransposons. First, it indicates that the lineage of elements leading to vertebrate retroviruses acquired a new RNH domain either from non-LTR retrotransposons or from a eukaryotic host genome. The preexisting retroviral RNH domain degenerated to become the tether (connection) domain of the reverse transcriptase (RT)-RNH complex. Second, it indicates that all LTR retrotransposons arose in eukaryotes well after the origin of the non-LTR retrotransposons. Because of the younger age of the LTR retrotransposons, their complex structure, and the absence of any prokaryotic precursors, we propose that the LTR retrotransposons originated as a fusion between a DNA-mediated transposon and a non-LTR retrotransposon. The resulting two-step mechanism of LTR retrotransposition, in which RNA is reverse transcribed away from the chromosomal target site, rather than directly onto the target site, was probably an adaptation to the uncoupling of transcription and translation in eukaryotic cells.

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“…Many of these clades contain ORF1p proteins that are unrelated to mammalian L1ORF1p but have similar functional properties (25)(26)(27)(28)(29). These proteins frequently contain CCHC zinc knuckles that are also found in the retroviral nucleocapsid protein Gag (30). This has fueled speculations on a more general functional (25,26,31) and structural (27,28) similarity between NLR ORF1p and retroviral nucleocapsid proteins.…”

mentioning

confidence: 99%

Non-LTR retrotransposons encode noncanonical RRM domains in their first open reading frame

Khazina

Weichenrieder

2009

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

135

200

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Non-LTR retrotransposons (NLRs) are a unique class of mobile genetic elements that have significant impact on the evolution of eukaryotic genomes. However, the molecular details and functions of their encoded proteins, in particular of the accessory ORF1p proteins, are poorly understood. Here, we identify noncanonical RNA-recognitionmotifs (RRMs) in several phylogenetically unrelated NLR ORF1p proteins. This provides an explanation for their RNA-binding properties and clearly shows that they are not related to the retroviral nucleocapsid protein Gag, despite the frequent presence of CCHC zinc knuckles. In particular, we characterize the ORF1p protein of the human long interspersed nuclear element 1 (LINE-1 or L1). We show that L1ORF1p is a multidomain protein, consisting of a coiled coil (cc), RRM, and C-terminal domain (CTD). Most importantly, we solved the crystal structure of the RRM domain, which is characterized by extended loops stabilized by unique salt bridges. Furthermore, we demonstrate that L1ORF1p trimerizes via its N-terminal cc domain, and we suggest that this property is functionally important for all homologues. The formation of distinct complexes with singlestranded nucleic acids requires the presence of the RRM and CTD domains on the same polypeptide chain as well as their close cooperation. Finally, the phylogenetic analysis of mammalian L1ORF1p shows an ancient origin of the RRM domain and supports a modular evolution of NLRs.genome evolution ͉ LINE-1 ͉ nucleic acid chaperone ͉ RNP ͉ crystal structure

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Transposable elements controlling I-R hybrid dysgenesis in D. melanogaster are similar to mammalian LINEs

Cited by 238 publications

References 54 publications

Nimbus (BgI): An active non-LTR retrotransposon of the Schistosoma mansoni snail host Biomphalaria glabrata

Nimbus (BgI): An active non-LTR retrotransposon of the Schistosoma mansoni snail host Biomphalaria glabrata

Phylogenetic Analysis of Ribonuclease H Domains Suggests a Late, Chimeric Origin of LTR Retrotransposable Elements and Retroviruses

Non-LTR retrotransposons encode noncanonical RRM domains in their first open reading frame

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