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In-vitro dual binding activity of a evolutionarily related subgroup of hnRNP proteins

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Abstract

The wide family of heterogeneous nuclear ribonucleoproteins (hnRNPs) comprises members that interact with single-stranded nucleic acids. On the basis of their structure, some of them are characterised by a tandem RNA-binding domain (RBD) and a glycine-rich C-terminus, showing a high degree of homology. Recently, we have isolated some proteins belonging to this group that interact with single-stranded cytosine-block telomeric DNA. The aim of the present investigation is to better characterise the relationship of some structural features shared by these proteins and their in-vitro interaction with the telomeric type sequences. We analysed the in-vitro binding properties of some of these components toward both single-stranded telomeric motifs. Using deletion mutants, the relationship between cytosine-rich motif binding activity and the structural features of one of these proteins is further characterized. This binding activity appears to be related to a subgroup of the 2xRBD+Glycine rich hnRNP, suggesting functionally distinct properties of these proteins, in agreement with their evolutionary relationship. (Mol Cell Biochem 268: 121–127, 2005)

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Author notes

  1. A. Akintunde Akindahunsi

    Present address: Department of Biochemistry, Federal University of Technology, via L. Giorgieri, P.M.B 704, Akure, Nigeria

Authors and Affiliations

  1. Department of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, via L. Giorgieri, 1, 34127, Trieste, Italy

    Antonella Bandiera, Nevenka Medic, A. Akintunde Akindahunsi & Giorgio Manzini

Authors
  1. Antonella Bandiera
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  2. Nevenka Medic
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  3. A. Akintunde Akindahunsi
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  4. Giorgio Manzini
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Bandiera, A., Medic, N., Akindahunsi, A.A. et al. In-vitro dual binding activity of a evolutionarily related subgroup of hnRNP proteins. Mol Cell Biochem 268, 121–127 (2005). https://doi.org/10.1007/s11010-005-3700-1

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  • DOI: https://doi.org/10.1007/s11010-005-3700-1

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