Interaction between trichosanthin, a ribosome-inactivating protein, and the ribosomal stalk protein P2 by chemical shift perturbation and mutagenesis analyses.

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Author(s): Chan DS;Chan DS; Chu LO; Lee KM; Too PH; Ma KW; Sze KH; Zhu G; Shaw PC; Wong KB
Source:
Nucleic acids research [Nucleic Acids Res] 2007; Vol. 35 (5), pp. 1660-72. Date of Electronic Publication: 2007 Feb 18.
Publication Type:
Journal Article; Research Support, Non-U.S. Gov't
Language:
English

Additional Information
- Source:
  Publisher: Oxford University Press Country of Publication: England NLM ID: 0411011 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1362-4962 (Electronic) Linking ISSN: 03051048 NLM ISO Abbreviation: Nucleic Acids Res Subsets: MEDLINE
- Publication Information:
  Publication: 1992- : Oxford : Oxford University Press
  Original Publication: London, Information Retrieval ltd.
- Subject Terms:
  Phosphoproteins/*chemistry ; Ribosomal Proteins/*chemistry ; Trichosanthin/*chemistry; Alanine/genetics ; Amino Acid Motifs ; Amino Acid Sequence ; Amino Acid Substitution ; Binding Sites ; Conserved Sequence ; Models, Molecular ; Mutagenesis ; Nuclear Magnetic Resonance, Biomolecular ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Protein Biosynthesis/drug effects ; Protein Structure, Tertiary ; Ribosomal Proteins/genetics ; Ribosomal Proteins/metabolism ; Sequence Deletion ; Trichosanthin/genetics ; Trichosanthin/pharmacology
- Abstract:
  Trichosanthin (TCS) is a type I ribosome-inactivating protein that inactivates ribosome by enzymatically depurinating the A(4324) at the alpha-sarcin/ricin loop of 28S rRNA. We have shown in this and previous studies that TCS interacts with human acidic ribosomal proteins P0, P1 and P2, which constitute the lateral stalk of eukaryotic ribosome. Deletion mutagenesis showed that TCS interacts with the C-terminal tail of P2, the sequences of which are conserved in P0, P1 and P2. The P2-binding site on TCS was mapped to the C-terminal domain by chemical shift perturbation experiments. Scanning charge-to-alanine mutagenesis has shown that K173, R174 and K177 in the C-terminal domain of TCS are involved in interacting with the P2, presumably through forming charge-charge interactions to the conserved DDD motif at the C-terminal tail of P2. A triple-alanine variant K173A/R174A/K177A of TCS, which fails to bind P2 and ribosomal stalk in vitro, was found to be 18-fold less active in inhibiting translation in rabbit reticulocyte lysate, suggesting that interaction with P-proteins is required for full activity of TCS. In an analogy to the role of stalk proteins in binding elongation factors, we propose that interaction with acidic ribosomal stalk proteins help TCS to locate its RNA substrate.
- References:
  J Biol Chem. 1995 May 26;270(21):12933-40. (PMID: 7759553)
  Nucleic Acids Res. 1994 Nov 11;22(22):4673-80. (PMID: 7984417)
  J Biomol NMR. 1995 Nov;6(3):277-93. (PMID: 8520220)
  J Mol Biol. 1996 Jul 19;260(3):289-98. (PMID: 8757792)
  J Biol Chem. 1997 Feb 7;272(6):3302-8. (PMID: 9013569)
  Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):905-21. (PMID: 9757107)
  J Biol Chem. 1999 Feb 5;274(6):3859-64. (PMID: 9920941)
  J Biol Chem. 1999 Sep 24;274(39):27578-82. (PMID: 10488095)
  Toxicon. 2005 May;45(6):683-9. (PMID: 15804517)
  Cell. 2005 Jul 1;121(7):991-1004. (PMID: 15989950)
  J Biol Chem. 2000 Feb 4;275(5):3382-90. (PMID: 10652330)
  FEBS Lett. 2000 Mar 31;470(3):239-43. (PMID: 10745075)
  EMBO J. 2000 Jun 1;19(11):2710-8. (PMID: 10835368)
  Science. 2000 Aug 11;289(5481):905-20. (PMID: 10937989)
  Eur J Biochem. 2001 Apr;268(7):2107-12. (PMID: 11277934)
  J Biol Chem. 2001 Jun 29;276(26):24075-81. (PMID: 11313342)
  Biochemistry. 2001 Aug 7;40(31):9104-14. (PMID: 11478877)
  Proc Natl Acad Sci U S A. 2001 Aug 28;98(18):10037-41. (PMID: 11517324)
  J Biol Chem. 2002 Feb 8;277(6):3857-62. (PMID: 11729183)
  Int J Biochem Cell Biol. 2002 Aug;34(8):911-5. (PMID: 12007628)
  EMBO J. 2004 Mar 10;23(5):1008-19. (PMID: 14976550)
  Genome Res. 2004 Jun;14(6):1188-90. (PMID: 15173120)
  Methods Mol Biol. 2004;278:313-52. (PMID: 15318002)
  Biochem J. 1973 Nov;136(3):813-5. (PMID: 4360718)
  J Biochem. 1985 Dec;98(6):1427-31. (PMID: 4093437)
  Eur J Biochem. 1986 Nov 17;161(1):111-7. (PMID: 3780730)
  J Biol Chem. 1987 Apr 25;262(12):5908-12. (PMID: 3571242)
  J Biol Chem. 1987 Jun 15;262(17):8128-30. (PMID: 3036799)
  Nucleic Acids Res. 1988 Feb 25;16(4):1349-57. (PMID: 3347493)
  J Biol Chem. 1988 Jun 25;263(18):8735-9. (PMID: 3288622)
  Biochemistry. 1989 Jul 25;28(15):6150-6. (PMID: 2675964)
  J Biol Chem. 1990 Jan 5;265(1):89-95. (PMID: 1688437)
  Nucleic Acids Res. 1990 Oct 25;18(20):6097-100. (PMID: 2172928)
  Nucleic Acids Res. 1992 Mar 25;20(6):1271-5. (PMID: 1561083)
  Int J Pept Protein Res. 1992 Jan;39(1):77-81. (PMID: 1634332)
  J Biol Chem. 1992 Sep 25;267(27):19179-85. (PMID: 1527039)
  J Mol Biol. 1992 Oct 20;227(4):1136-45. (PMID: 1433290)
  Eur J Biochem. 1994 Apr 15;221(2):787-91. (PMID: 8174558)
  Nat Struct Biol. 1994 Oct;1(10):695-700. (PMID: 7634073)
- Accession Number:
  0 (Phosphoproteins)
  0 (Ribosomal Proteins)
  0 (phosphoprotein P2, ribosomal)
  60318-52-7 (Trichosanthin)
  OF5P57N2ZX (Alanine)
- Publication Date:
  Date Created: 20070220 Date Completed: 20070430 Latest Revision: 20181113
- Publication Date:
  20231215
- Accession Number:
  PMC1865052
- Accession Number:
  10.1093/nar/gkm065
- Accession Number:
  17308345

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