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The action mode of the ribosome-inactivating protein α-sarcin

  • Original Paper
  • Published:
Journal of Biomedical Science

Abstract

Based on the tertiary structure of the ribosome-inactivating protein α-sarcin, domains that are responsible for hydrolyzing ribosomes and naked RNA have been dissected. In this study, we found that the head-to-tail interaction between the first amino β-strand and the last carboxyl β-strand is not involved in catalyzing the hydrolysis of ribosomes or ribonucleic acids. Instead, a four-strand pleated β-sheet is indispensable for catalyzing both substrates, suggesting that α-sarcin and ribonuclease T1 (RNase T1) share a similar catalytic center. The integrity of an amino β-hairpin and that of the loop L3 in α-sarcin are crucial for recognizing and hydrolyzing ribosomes in vitro and in vivo. However, a mutant protein without the β-hairpin structure, or with a disrupted loop L3, is still capable of digesting ribonucleic acids. The functional involvement of the β-hairpin and the loop L3 in the sarcin stem/loop RNA of ribosomes is demonstrated by a docking model, suggesting that the two structures are in essence naturally designed to distinguish ribosome-inactivating proteins from RNase T1 to inactivate ribosomes.

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Authors and Affiliations

  1. Institute of Microbiology and Immunology, National Yang-Ming University, Taipei, Taiwan, ROC

    Luen Hwu

  2. Institute of Genetics, National Yang-Ming University Shih-Pai, Taipei 112, Taiwan

    Kuan-Chun Huang, Dow-Tien Chen &  Alan Lin

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  1. Luen Hwu
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Hwu, L., Huang, KC., Chen, DT. et al. The action mode of the ribosome-inactivating protein α-sarcin. J Biomed Sci 7, 420–428 (2000). https://doi.org/10.1007/BF02255817

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