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The Ribosomal Protein RpL22 Interacts In Vitro with 5'-UTR Sequences Found in Some Drosophila melanogaster Transposons.
Minervini, Crescenzio Francesco; Berloco, Maria Francesca; Marsano, René Massimiliano; Viggiano, Luigi.
Afiliação
  • Minervini CF; Department of Emergency and Organ Transplantation (D.E.T.O.), Hematology and Stem Cell Transplantation Unit, University of Bari "Aldo Moro", 70124 Bari, Italy.
  • Berloco MF; Department of Biology, Università degli Studi di Bari "Aldo Moro", 70125 Bari, Italy.
  • Marsano RM; Department of Biology, Università degli Studi di Bari "Aldo Moro", 70125 Bari, Italy.
  • Viggiano L; Department of Genetics Anthropology Evolution, University of Parma, Parco Area delle Scienze 11/A, 43124 Parma, Italy.
Genes (Basel) ; 13(2)2022 02 05.
Article em En | MEDLINE | ID: mdl-35205350
ABSTRACT
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 gypsy and Idefix, and the enhancer of ZAM of Drosophila melanogaster. Recently we have shown that in the 5'-UTR of the LTR-retrotransposon ZAM there is a sequence structured in tandem-repeat capable of operating as an insulator both in Drosophila (S2R+) 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 D. melanogaster ribosomal protein RpL22. The Drosophila 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 Drosophila. In this paper, we show, by two independent sets of experiments, that DmRpL22 is able to directly and specifically bind DNA of Drosophila melanogaster.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Drosophila / Drosophila melanogaster Limite: Animals / Humans Idioma: En Revista: Genes (Basel) Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Itália

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Drosophila / Drosophila melanogaster Limite: Animals / Humans Idioma: En Revista: Genes (Basel) Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Itália
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