A self-encoded capsid derivative restricts Ty1 retrotransposition in Saccharomyces

Garfinkel, David; Tucker, Jessica M.; Saha, Agniva; Nishida, Yuya; Pachulska-Wieczorek, Katarzyna; Błaszczyk, Leszek; Purzycka, Katarzyna J.

doi:10.1007/s00294-015-0550-6

Cited by 28 publications

(25 citation statements)

References 78 publications

(121 reference statements)

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“…Furthermore, it has been shown that proteolytic processing of the Gag protein of S . cerevisiae Ty1 transposable elements that assemble in the cytoplasm is also required for reverse transcription and transposition activity [67, 68]. Although we cannot rule out that in FVs Env binding to Gag might be a trigger to conformational rearrangement, we suggest that Gag cleavage to form p68, initiates the rearrangement of Gag, resulting in the appearance of the discrete capsid layer observed by cEM.…”

Section: Discussionmentioning

confidence: 96%

Structure of a Spumaretrovirus Gag Central Domain Reveals an Ancient Retroviral Capsid

et al. 2016

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The Spumaretrovirinae, or foamy viruses (FVs) are complex retroviruses that infect many species of monkey and ape. Despite little sequence homology, FV and orthoretroviral Gag proteins perform equivalent functions, including genome packaging, virion assembly, trafficking and membrane targeting. However, there is a paucity of structural information for FVs and it is unclear how disparate FV and orthoretroviral Gag molecules share the same function. To probe the functional overlap of FV and orthoretroviral Gag we have determined the structure of a central region of Gag from the Prototype FV (PFV). The structure comprises two all α-helical domains NtDCEN and CtDCEN that although they have no sequence similarity, we show they share the same core fold as the N- (NtDCA) and C-terminal domains (CtDCA) of archetypal orthoretroviral capsid protein (CA). Moreover, structural comparisons with orthoretroviral CA align PFV NtDCEN and CtDCEN with NtDCA and CtDCA respectively. Further in vitro and functional virological assays reveal that residues making inter-domain NtDCEN—CtDCEN interactions are required for PFV capsid assembly and that intact capsid is required for PFV reverse transcription. These data provide the first information that relates the Gag proteins of Spuma and Orthoretrovirinae and suggests a common ancestor for both lineages containing an ancient CA fold.

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Section: Discussionmentioning

confidence: 96%

Structure of a Spumaretrovirus Gag Central Domain Reveals an Ancient Retroviral Capsid

et al. 2016

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“…The relationship between altered Ty1 retromobility and altered Ty1i regulation reported here and the CNC phenomenon, in which increased Ty1 copy number leads to increased Ty1i expression[22,25], remains to be explored. It will be interesting to determine the molecular mechanism underlying CNC and the specific role that promoter competition and Mediator complex plays in this phenomenon.…”

Section: Discussionmentioning

confidence: 99%

“…Ty1 relies extensively on autoregulatory factors and host factors to successfully complete its mobility cycle and limit its mobility so as not to destabilize the host genome [18,22]. One mechanism of auto-inhibition known as copy number control (CNC) is defined by a copy number-dependent decrease in Ty1 retrotransposition observed both in S. cerevisiae and its close relative, S. paradoxus [23–25].…”

Section: Introductionmentioning

confidence: 99%

The Mediator co-activator complex regulates Ty1 retromobility by controlling the balance between Ty1i and Ty1 promoters

Salinero

Knoll

Zhu

et al. 2017

Preprint

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4The Ty1 retrotransposons present in the genome of Saccharomyces cerevisiae belong to the large class 3 5 of mobile genetic elements that replicate via an RNA intermediary and constitute a significant portion of 3 6 most eukaryotic genomes. The retromobility of Ty1 is regulated by numerous host factors, including 3 7 several subunits of the Mediator transcriptional co-activator complex. In spite of its known function in 3 8 the nucleus, previous studies have implicated Mediator in the regulation of post-translational steps in 3 9 Ty1 retromobility. To resolve this paradox, we systematically examined the effects of deleting non-4 0 essential Mediator subunits on the frequency of Ty1 retromobility and levels of retromobility 4 1 intermediates. Our findings reveal that loss of distinct Mediator subunits alters Ty1 retromobility 4 2 positively or negatively over a >10,000-fold range by regulating the ratio of an internal transcript, Ty1i, 4 3 to the genomic Ty1 transcript. Ty1i RNA encodes a dominant negative inhibitor of Ty1 retromobility 4 4 that blocks virus-like particle maturation and cDNA synthesis. These results resolve the conundrum of 4 5

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“…Importantly, none of those systems operate natively in S. cerevisiae or its sister species, S. paradoxus (Drinnenberg et al 2009). Instead, Ty1 mobility in S. cerevisiae and S. paradoxus is limited by a novel retroelement-directed restriction mechanism termed Copy Number Control (CNC) (Wilke et al 1992; Garfinkel et al 2003; Saha et al 2015; Garfinkel et al 2016; Ahn et al 2017). CNC is defined as a decrease in Ty1 mobility when additional copies of the Ty1 element are present in the genome.…”

Section: Introductionmentioning

confidence: 99%

Evolution of Ty1 copy number control in yeast by horizontal transfer of agaggene

Czaja

Bensasson

Ahn

et al. 2019

Preprint

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Insertion of mobile DNA sequences typically has deleterious effects on host fitness, and thus diverse mechanisms have evolved to control mobile element proliferation across the tree of life. Mobility of the Ty1 retrotransposon in Saccharomyces yeasts is regulated by a novel form of copy number control (CNC) mediated by a self-encoded restriction factor derived from the Ty1 gag capsid gene that inhibits virus-like particle function. Here, we survey a panel of wild and human-associated strains of S. cerevisiae and S. paradoxus to investigate how genomic Ty1 content influences variation in Ty1 mobility. We observe high levels of mobility for a canonical Ty1 tester element in permissive strains that either lack full-length Ty1 elements or only contain full-length copies of the Ty1’ subfamily that have a divergent gag sequence. In contrast, low levels of canonical Ty1 mobility are observed in restrictive strains carrying full-length Ty1 elements containing canonical gag. Phylogenomic analysis of full-length Ty1 elements revealed that Ty1’ is the ancestral subfamily present in wild strains of S. cerevisiae, and that canonical Ty1 in S. cerevisiae is a derived subfamily that acquired gag from S. paradoxus by horizontal transfer and recombination. Our results provide evidence that variation in the ability of S. cerevisiae and S. paradoxus strains to repress canonical Ty1 transposition via CNC is encoded by the genomic content of different Ty1 subfamilies, and that self-encoded forms of transposon control can spread across species boundaries by horizontal transfer.

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A self-encoded capsid derivative restricts Ty1 retrotransposition in Saccharomyces

Cited by 28 publications

References 78 publications

Structure of a Spumaretrovirus Gag Central Domain Reveals an Ancient Retroviral Capsid

Structure of a Spumaretrovirus Gag Central Domain Reveals an Ancient Retroviral Capsid

The Mediator co-activator complex regulates Ty1 retromobility by controlling the balance between Ty1i and Ty1 promoters

Evolution of Ty1 copy number control in yeast by horizontal transfer of agaggene

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