Literature DB >> 14675755

RALyase; a terminator of elongation function of depurinated ribosomes.

Akihiko Ozawa1, Tatsuya Sawasaki, Kazuyuki Takai, Toshio Uchiumi, Hiroyuki Hori, Yaeta Endo.   

Abstract

Plant ribosomal RNA apurinic site specific lyase (RALyase) cleaves the phosphodiester bond at the depurinated site produced by ribosome-inactivating protein, while the biological role of this enzyme is not clear. As the depurinated ribosomes retain weak translation elongation activities, it was suggested that RALyase completes the ribosome inactivation. To confirm this point, we measured the effects of the phosphodiester cleavage using a fusion of wheat RALyase produced with a cell-free protein synthesis system from wheat germ. The results indicated that RALyase diminishes the residual elongation activities of the depurinated ribosomes.

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Year:  2003        PMID: 14675755     DOI: 10.1016/s0014-5793(03)01304-8

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  The chemical stability of abasic RNA compared to abasic DNA.

Authors:  Pascal A Küpfer; Christian J Leumann
Journal:  Nucleic Acids Res       Date:  2006-12-06       Impact factor: 16.971

Review 2.  Extensive Evolution of Cereal Ribosome-Inactivating Proteins Translates into Unique Structural Features, Activation Mechanisms, and Physiological Roles.

Authors:  Jeroen De Zaeytijd; Els J M Van Damme
Journal:  Toxins (Basel)       Date:  2017-03-29       Impact factor: 4.546

3.  Trans-lesion synthesis and RNaseH activity by reverse transcriptases on a true abasic RNA template.

Authors:  Pascal A Küpfer; Caroline Crey-Desbiolles; Christian J Leumann
Journal:  Nucleic Acids Res       Date:  2007-10-11       Impact factor: 16.971

  3 in total

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