Reliance of Host-Encoded Regulators of Retromobility on Ty1 Promoter Activity or Architecture

Salinero, Alicia C.; Emerson, Simey; Cormier, Tayla C.; Yin, John; Morse, Randall H.; Curcio, M. Joan

doi:10.3389/fmolb.2022.896215

Cited by 3 publications

(2 citation statements)

References 87 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…S4A and S4B). Moreover, this promoter has a relatively weak activity (56) such that in WT cells the retrotransposition frequency of Ty1- his3AI expressed from the PSP2 promoter was of the same order of magnitude as that obtained with a Ty1- his3AI chromosomal element expressed from the Ty1 promoter (Compare WT in Fig. 3A and Fig.…”

Section: Resultsmentioning

confidence: 86%

A proteomic screen of Ty1 integrase partners identifies the protein kinase CK2 as a regulator of Ty1 retrotransposition

Barkova

Adhya

Conesa

et al. 2022

Preprint

View full text Add to dashboard Cite

Background Transposable elements are ubiquitous and play a fundamental role in shaping genomes during evolution. Since excessive transposition can be mutagenic, mechanisms exist in the cells to keep these mobile elements under control. Although many cellular factors regulating the mobility of the retrovirus-like transposon Ty1 in Saccharomyces cerevisiae have been identified in genetic screens, only very few of them interact physically with Ty1 integrase (IN). Results Here, we perform a proteomic screen to establish Ty1 IN interactome. Among the 265 potential interacting partners, we focus our study on the conserved CK2 kinase. We confirm the interaction between IN and CK2, demonstrate that IN is a substrate of CK2 in vitro and identify the modified residues. We find that Ty1 IN is phosphorylated in vivo and that these modifications are dependent in part on CK2. No significant change in Ty1 retromobility could be observed when we introduce phospho-ablative mutations that prevent IN phosphorylation by CK2 in vitro. However, the absence of CK2 holoenzyme results in a strong stimulation of Ty1 retrotransposition, characterized by an increase in Ty1 mRNA and protein levels and a high accumulation of cDNA. Conclusion Our study highlights an important role of CK2 in the regulation of Ty1 retrotransposition. We provide the first evidence that Ty1 IN is post-translationally modified in vivo, as observed for retroviral INs, and demonstrate that CK2 strongly represses Ty1 mobility by inhibiting Ty1 transcription. The proteomic approach enabled the identification of many new Ty1 IN interacting partners, whose potential role in the control of Ty1 mobility will be interesting to study.

show abstract

Section: Resultsmentioning

confidence: 86%

A proteomic screen of Ty1 integrase partners identifies the protein kinase CK2 as a regulator of Ty1 retrotransposition

Barkova

Adhya

Conesa

et al. 2022

Preprint

View full text Add to dashboard Cite

show abstract

“…S4A and S4B). Moreover, this promoter has a relatively weak activity (57) such that in WT cells the retrotransposition frequency of Ty1-his3AI expressed from the PSP2 promoter was of the same order of magnitude as that obtained with a Ty1-his3AI chromosomal element expressed from the Ty1 promoter (Compare WT in Fig. 3A and Fig.…”

Section: In Is Phosphorylated During Ty1 Replicationmentioning

confidence: 79%

A proteomic screen of Ty1 integrase partners identifies the protein kinase CK2 as a regulator of Ty1 retrotransposition

Barkova

Adhya

Conesa

et al. 2022

Preprint

View full text Add to dashboard Cite

Background. Transposable elements are ubiquitous and play a fundamental role in shaping genomes during evolution. Since excessive transposition can be mutagenic, mechanisms exist in the cells to keep these mobile elements under control. Although many cellular factors regulating the mobility of the retrovirus-like transposon Ty1 in Saccharomyces cerevisiae have been identified in genetic screens, only very few of them interact physically with Ty1 integrase (IN).Results. Here, we perform a proteomic screen to establish Ty1 IN interactome. Among the 265 potential interacting partners, we focus our study on the conserved CK2 kinase. We confirm the interaction between IN and CK2, demonstrate that IN is a substrate of CK2 in vitro and identify the modified residues. We find that Ty1 IN is phosphorylated in vivo and that these modifications are dependent in part on CK2. No significant change in Ty1 retromobility could be observed when we introduce phospho-ablative mutations that prevent IN phosphorylation by CK2 in vitro. However, the absence of CK2 holoenzyme results in a strong stimulation of Ty1 retrotransposition, characterized by an increase in Ty1 mRNA and protein levels and a high accumulation of cDNA. ConclusionOur study highlights an important role of CK2 in the regulation of Ty1 retrotransposition. We provide the first evidence that Ty1 IN is post-translationally modified in vivo, as observed for retroviral INs, and demonstrate that CK2 strongly represses Ty1 mobility by inhibiting Ty1 transcription. The proteomic approach enabled the identification of many new Ty1 IN interacting partners, whose potential role in the control of Ty1 mobility will be interesting to study.

show abstract

A proteomic screen of Ty1 integrase partners identifies the protein kinase CK2 as a regulator of Ty1 retrotransposition

et al. 2022

View full text Add to dashboard Cite

Background Transposable elements are ubiquitous and play a fundamental role in shaping genomes during evolution. Since excessive transposition can be mutagenic, mechanisms exist in the cells to keep these mobile elements under control. Although many cellular factors regulating the mobility of the retrovirus-like transposon Ty1 in Saccharomyces cerevisiae have been identified in genetic screens, only very few of them interact physically with Ty1 integrase (IN). Results Here, we perform a proteomic screen to establish Ty1 IN interactome. Among the 265 potential interacting partners, we focus our study on the conserved CK2 kinase. We confirm the interaction between IN and CK2, demonstrate that IN is a substrate of CK2 in vitro and identify the modified residues. We find that Ty1 IN is phosphorylated in vivo and that these modifications are dependent in part on CK2. No significant change in Ty1 retromobility could be observed when we introduce phospho-ablative mutations that prevent IN phosphorylation by CK2 in vitro. However, the absence of CK2 holoenzyme results in a strong stimulation of Ty1 retrotransposition, characterized by an increase in Ty1 mRNA and protein levels and a high accumulation of cDNA. Conclusion Our study shows that Ty1 IN is phosphorylated, as observed for retroviral INs and highlights an important role of CK2 in the regulation of Ty1 retrotransposition. In addition, the proteomic approach enabled the identification of many new Ty1 IN interacting partners, whose potential role in the control of Ty1 mobility will be interesting to study.

show abstract

Reliance of Host-Encoded Regulators of Retromobility on Ty1 Promoter Activity or Architecture

Cited by 3 publications

References 87 publications

A proteomic screen of Ty1 integrase partners identifies the protein kinase CK2 as a regulator of Ty1 retrotransposition

A proteomic screen of Ty1 integrase partners identifies the protein kinase CK2 as a regulator of Ty1 retrotransposition

A proteomic screen of Ty1 integrase partners identifies the protein kinase CK2 as a regulator of Ty1 retrotransposition

A proteomic screen of Ty1 integrase partners identifies the protein kinase CK2 as a regulator of Ty1 retrotransposition

Contact Info

Product

Resources

About