Literature DB >> 16126173

Ribosomal protein L10a, a bridge between trichosanthin and the ribosome.

Xuechun Xia1, Fajian Hou, Jie Li, Huiling Nie.   

Abstract

Trichosanthin is a type I ribosome-inactivating protein with many pharmacological activities. The trichosanthin-coupled Sepharose affinity purification revealed a protein, which was identified by mass spectrometry as the ribosomal protein L10a. The interaction between trichosanthin and recombinant L10a was further confirmed by in vitro binding assay. Kinetic analysis by surface plasmon resonance technology revealed that L10a had a high affinity to trichosanthin with a K(D) of 7.78nM. The study with mutated forms of trichosanthin demonstrated that this specific association correlates with the ribosome-inactivating activity of trichosanthin. This finding might provide insight into the mechanisms by which trichosanthin inactivates ribosome and that underlies its pharmacological effect.

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Year:  2005        PMID: 16126173     DOI: 10.1016/j.bbrc.2005.08.074

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Characterization and biological activity of the ribosomal protein L10a of the white shrimp: Fenneropenaeus merguiensis De Man during vitellogenesis.

Authors:  Monwadee Wonglapsuwan; Teruo Miyazaki; Wiriya Loongyai; Wilaiwan Chotigeat
Journal:  Mar Biotechnol (NY)       Date:  2009-08-21       Impact factor: 3.619

2.  The C-terminal fragment of the ribosomal P protein complexed to trichosanthin reveals the interaction between the ribosome-inactivating protein and the ribosome.

Authors:  Priscilla Hiu-Mei Too; Meiji Kit-Wan Ma; Amanda Nga-Sze Mak; Yuen-Ting Wong; Christine Kit-Ching Tung; Guang Zhu; Shannon Wing-Ngor Au; Kam-Bo Wong; Pang-Chui Shaw
Journal:  Nucleic Acids Res       Date:  2008-12-10       Impact factor: 16.971

  2 in total

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