Abstract
The yeast Ty5 retrotransposon preferentially integrates into heterochromatin at the telomeres and silent mating loci. Target specificity is mediated by a small domain of Ty5 integrase (the targeting domain, TD), which interacts with the heterochromatin protein Sir4 and tethers the integration complex to target sites. Here we demonstrate that TD is phosphorylated and that phosphorylation is required for interaction with Sir4. The yeast cell, therefore, through posttranslational modification, controls Ty5's mutagenic potential: when TD is phosphorylated, insertions occur in gene-poor heterochromatin, thereby minimizing deleterious consequences of transposition; however, in the absence of phosphorylation, Ty5 integrates throughout the genome, frequently causing mutations. TD phosphorylation is reduced under stress conditions, specifically starvation for amino acids, nitrogen, or fermentable carbon. This suggests that Ty5 target specificity changes in response to nutrient availability and is consistent with McClintock's hypothesis that mobile elements restructure host genomes as an adaptive response to environmental challenge.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 289-299 |
| Number of pages | 11 |
| Journal | Molecular Cell |
| Volume | 27 |
| Issue number | 2 |
| DOIs | |
| State | Published - Jul 20 2007 |
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Phosphorylation Regulates Integration of the Yeast Ty5 Retrotransposon into Heterochromatin. / Dai, Junbiao; Xie, Weiwu; Brady, Troy L.; Gao, Jiquan; Voytas, Daniel F.
In: Molecular Cell, Vol. 27, No. 2, 20.07.2007, p. 289-299.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Phosphorylation Regulates Integration of the Yeast Ty5 Retrotransposon into Heterochromatin
AU - Dai, Junbiao
AU - Xie, Weiwu
AU - Brady, Troy L.
AU - Gao, Jiquan
AU - Voytas, Daniel F.
PY - 2007/7/20
Y1 - 2007/7/20
N2 - The yeast Ty5 retrotransposon preferentially integrates into heterochromatin at the telomeres and silent mating loci. Target specificity is mediated by a small domain of Ty5 integrase (the targeting domain, TD), which interacts with the heterochromatin protein Sir4 and tethers the integration complex to target sites. Here we demonstrate that TD is phosphorylated and that phosphorylation is required for interaction with Sir4. The yeast cell, therefore, through posttranslational modification, controls Ty5's mutagenic potential: when TD is phosphorylated, insertions occur in gene-poor heterochromatin, thereby minimizing deleterious consequences of transposition; however, in the absence of phosphorylation, Ty5 integrates throughout the genome, frequently causing mutations. TD phosphorylation is reduced under stress conditions, specifically starvation for amino acids, nitrogen, or fermentable carbon. This suggests that Ty5 target specificity changes in response to nutrient availability and is consistent with McClintock's hypothesis that mobile elements restructure host genomes as an adaptive response to environmental challenge.
AB - The yeast Ty5 retrotransposon preferentially integrates into heterochromatin at the telomeres and silent mating loci. Target specificity is mediated by a small domain of Ty5 integrase (the targeting domain, TD), which interacts with the heterochromatin protein Sir4 and tethers the integration complex to target sites. Here we demonstrate that TD is phosphorylated and that phosphorylation is required for interaction with Sir4. The yeast cell, therefore, through posttranslational modification, controls Ty5's mutagenic potential: when TD is phosphorylated, insertions occur in gene-poor heterochromatin, thereby minimizing deleterious consequences of transposition; however, in the absence of phosphorylation, Ty5 integrates throughout the genome, frequently causing mutations. TD phosphorylation is reduced under stress conditions, specifically starvation for amino acids, nitrogen, or fermentable carbon. This suggests that Ty5 target specificity changes in response to nutrient availability and is consistent with McClintock's hypothesis that mobile elements restructure host genomes as an adaptive response to environmental challenge.
KW - DNA
UR - http://www.scopus.com/inward/record.url?scp=34447328702&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=34447328702&partnerID=8YFLogxK
U2 - 10.1016/j.molcel.2007.06.010
DO - 10.1016/j.molcel.2007.06.010
M3 - Article
C2 - 17643377
AN - SCOPUS:34447328702
VL - 27
SP - 289
EP - 299
JO - Molecular Cell
JF - Molecular Cell
SN - 1097-2765
IS - 2
ER -