The Ribosomal Protein RpL22 Interacts In Vitro with 5′-UTR Sequences Found in Some <i>Drosophila melanogaster</i> Transposons
Mobility of eukaryotic transposable elements (TEs) are finely regulated to avoid an excessive mutational load caused by their movement. The transposition of retrotransposons is usually regulated through the interaction of host- and TE-encoded proteins, with non-coding regions (LTR and 5′-UTR) of the...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2022-02-01
|
| Series: | Genes |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2073-4425/13/2/305 |
| _version_ | 1797479872608600064 |
|---|---|
| author | Crescenzio Francesco Minervini Maria Francesca Berloco René Massimiliano Marsano Luigi Viggiano |
| author_facet | Crescenzio Francesco Minervini Maria Francesca Berloco René Massimiliano Marsano Luigi Viggiano |
| author_sort | Crescenzio Francesco Minervini |
| collection | DOAJ |
| description | Mobility of eukaryotic transposable elements (TEs) are finely regulated to avoid an excessive mutational load caused by their movement. The transposition of retrotransposons is usually regulated through the interaction of host- and TE-encoded proteins, with non-coding regions (LTR and 5′-UTR) of the transposon. Examples of new potent cis-acting sequences, identified and characterized in the non-coding regions of retrotransposons, include the insulator of <i>gypsy</i> and Idefix, and the enhancer of <i>ZAM</i> of <i>Drosophila melanogaster</i>. Recently we have shown that in the 5′-UTR of the LTR-retrotransposon <i>ZAM</i> there is a sequence structured in tandem-repeat capable of operating as an insulator both in <i>Drosophila</i> (S2R<sup>+</sup>) and human cells (HEK293). Here, we test the hypothesis that tandem repeated 5′-UTR of a different LTR-retrotransposon could accommodate similar regulatory elements. The comparison of the 5′-UTR of some LTR-transposons allowed us to identify a shared motif of 13 bp, called Transposable Element Redundant Motif (TERM). Surprisingly, we demonstrated, by Yeast One-Hybrid assay, that TERM interacts with the <i>D</i>. <i>melanogaster</i> ribosomal protein RpL22. The <i>Drosophila</i> RpL22 has additional Ala-, Lys- and Pro-rich sequences at the amino terminus, which resembles the carboxy-terminal portion of histone H1 and histone H5. For this reason, it has been hypothesized that RpL22 might have two functions, namely the role in organizing the ribosome, and a potential regulatory role involving DNA-binding similar to histone H1, which represses transcription in <i>Drosophila</i>. In this paper, we show, by two independent sets of experiments, that DmRpL22 is able to directly and specifically bind DNA of <i>Drosophila melanogaster</i>. |
| first_indexed | 2024-03-09T21:52:02Z |
| format | Article |
| id | doaj.art-999a7872693442e3adb756f0555e217a |
| institution | Directory Open Access Journal |
| issn | 2073-4425 |
| language | English |
| last_indexed | 2024-03-09T21:52:02Z |
| publishDate | 2022-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Genes |
| spelling | doaj.art-999a7872693442e3adb756f0555e217a2023-11-23T20:04:49ZengMDPI AGGenes2073-44252022-02-0113230510.3390/genes13020305The Ribosomal Protein RpL22 Interacts In Vitro with 5′-UTR Sequences Found in Some <i>Drosophila melanogaster</i> TransposonsCrescenzio Francesco Minervini0Maria Francesca Berloco1René Massimiliano Marsano2Luigi Viggiano3Department of Emergency and Organ Transplantation (D.E.T.O.), Hematology and Stem Cell Transplantation Unit, University of Bari “Aldo Moro”, 70124 Bari, ItalyDepartment of Biology, Università degli Studi di Bari “Aldo Moro”, 70125 Bari, ItalyDepartment of Biology, Università degli Studi di Bari “Aldo Moro”, 70125 Bari, ItalyDepartment of Biology, Università degli Studi di Bari “Aldo Moro”, 70125 Bari, ItalyMobility of eukaryotic transposable elements (TEs) are finely regulated to avoid an excessive mutational load caused by their movement. The transposition of retrotransposons is usually regulated through the interaction of host- and TE-encoded proteins, with non-coding regions (LTR and 5′-UTR) of the transposon. Examples of new potent cis-acting sequences, identified and characterized in the non-coding regions of retrotransposons, include the insulator of <i>gypsy</i> and Idefix, and the enhancer of <i>ZAM</i> of <i>Drosophila melanogaster</i>. Recently we have shown that in the 5′-UTR of the LTR-retrotransposon <i>ZAM</i> there is a sequence structured in tandem-repeat capable of operating as an insulator both in <i>Drosophila</i> (S2R<sup>+</sup>) and human cells (HEK293). Here, we test the hypothesis that tandem repeated 5′-UTR of a different LTR-retrotransposon could accommodate similar regulatory elements. The comparison of the 5′-UTR of some LTR-transposons allowed us to identify a shared motif of 13 bp, called Transposable Element Redundant Motif (TERM). Surprisingly, we demonstrated, by Yeast One-Hybrid assay, that TERM interacts with the <i>D</i>. <i>melanogaster</i> ribosomal protein RpL22. The <i>Drosophila</i> RpL22 has additional Ala-, Lys- and Pro-rich sequences at the amino terminus, which resembles the carboxy-terminal portion of histone H1 and histone H5. For this reason, it has been hypothesized that RpL22 might have two functions, namely the role in organizing the ribosome, and a potential regulatory role involving DNA-binding similar to histone H1, which represses transcription in <i>Drosophila</i>. In this paper, we show, by two independent sets of experiments, that DmRpL22 is able to directly and specifically bind DNA of <i>Drosophila melanogaster</i>.https://www.mdpi.com/2073-4425/13/2/305ribosomal proteinRpl22<i>Drosophila</i>DNA-protein interactiontransposable elementshistone 1-like |
| spellingShingle | Crescenzio Francesco Minervini Maria Francesca Berloco René Massimiliano Marsano Luigi Viggiano The Ribosomal Protein RpL22 Interacts In Vitro with 5′-UTR Sequences Found in Some <i>Drosophila melanogaster</i> Transposons Genes ribosomal protein Rpl22 <i>Drosophila</i> DNA-protein interaction transposable elements histone 1-like |
| title | The Ribosomal Protein RpL22 Interacts In Vitro with 5′-UTR Sequences Found in Some <i>Drosophila melanogaster</i> Transposons |
| title_full | The Ribosomal Protein RpL22 Interacts In Vitro with 5′-UTR Sequences Found in Some <i>Drosophila melanogaster</i> Transposons |
| title_fullStr | The Ribosomal Protein RpL22 Interacts In Vitro with 5′-UTR Sequences Found in Some <i>Drosophila melanogaster</i> Transposons |
| title_full_unstemmed | The Ribosomal Protein RpL22 Interacts In Vitro with 5′-UTR Sequences Found in Some <i>Drosophila melanogaster</i> Transposons |
| title_short | The Ribosomal Protein RpL22 Interacts In Vitro with 5′-UTR Sequences Found in Some <i>Drosophila melanogaster</i> Transposons |
| title_sort | ribosomal protein rpl22 interacts in vitro with 5 utr sequences found in some i drosophila melanogaster i transposons |
| topic | ribosomal protein Rpl22 <i>Drosophila</i> DNA-protein interaction transposable elements histone 1-like |
| url | https://www.mdpi.com/2073-4425/13/2/305 |
| work_keys_str_mv | AT crescenziofrancescominervini theribosomalproteinrpl22interactsinvitrowith5utrsequencesfoundinsomeidrosophilamelanogasteritransposons AT mariafrancescaberloco theribosomalproteinrpl22interactsinvitrowith5utrsequencesfoundinsomeidrosophilamelanogasteritransposons AT renemassimilianomarsano theribosomalproteinrpl22interactsinvitrowith5utrsequencesfoundinsomeidrosophilamelanogasteritransposons AT luigiviggiano theribosomalproteinrpl22interactsinvitrowith5utrsequencesfoundinsomeidrosophilamelanogasteritransposons AT crescenziofrancescominervini ribosomalproteinrpl22interactsinvitrowith5utrsequencesfoundinsomeidrosophilamelanogasteritransposons AT mariafrancescaberloco ribosomalproteinrpl22interactsinvitrowith5utrsequencesfoundinsomeidrosophilamelanogasteritransposons AT renemassimilianomarsano ribosomalproteinrpl22interactsinvitrowith5utrsequencesfoundinsomeidrosophilamelanogasteritransposons AT luigiviggiano ribosomalproteinrpl22interactsinvitrowith5utrsequencesfoundinsomeidrosophilamelanogasteritransposons |