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PMID: 2175904 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Eukaryotic initiation factor 3 is required for poliovirus 2A protease-induced cleavage of the p220 component of eukaryotic initiation factor 4F.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 87 ·No. 24 ·1990-12-00 ·Pages 9529-33

Wyckoff EE, Hershey JW, Ehrenfeld E

Abstract

After cultured cells are infected with poliovirus, cellular mRNA fails to bind to ribosomes, and synthesis of the majority of cellular proteins ceases. The defective step has been localized to the cap-dependent activity of the eukaryotic translation initiation factor 4F. Inactivation of this factor correlates with the cleavage of its largest subunit, p220, into characteristic products observed in infected cells. This cleavage is mediated by the poliovirus protease 2Apro. Previous work suggests that 2Apro does not catalyze the reaction directly, suggesting that one or more cellular proteins is required for the degradation of p220. To identify such a protein, we have developed an assay in which cleavage of a p220 substrate in the presence of poliovirus 2Apro is dependent upon the addition of HeLa cell proteins. By using this assay, we show that another factor, eukaryotic translation initiation factor 3, is required for 2Apro-dependent cleavage of p220.

MeSH Terms
Cysteine Endopeptidases/genetics,metabolism Escherichia coli/genetics Eukaryotic Initiation Factor-3 Eukaryotic Initiation Factor-4F HeLa Cells/metabolism Humans Macromolecular Substances Molecular Weight Peptide Initiation Factors/isolation & purification,metabolism Plasmids Poliovirus/enzymology,genetics Recombinant Fusion Proteins/metabolism Restriction Mapping Substrate Specificity Viral Proteins
Chemicals
Eukaryotic Initiation Factor-3 Eukaryotic Initiation Factor-4F Macromolecular Substances Peptide Initiation Factors Recombinant Fusion Proteins Viral Proteins Cysteine Endopeptidases picornain 2A, Picornavirus
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Wyckoff E E
Department of Biochemistry and Cellular, University of Utah School of Medicine, Salt Lake City 84132.
Hershey J W
Ehrenfeld E
References (37)
37 references, click to expand
  1. Association of cap-binding protein with eucaryotic initiation factor 3 in initiation factor preparations from uninfected and poliovirus-infected HeLa cells.
    J Virol. 1982 Apr;42(1):200-7 PMID: 6283140
  2. Two forms of purified m7G-cap binding protein with different effects on capped mRNA translation in extracts of uninfected and poliovirus-infected HeLa cells.
    J Biol Chem. 1981 Aug 10;256(15):7691-4 PMID: 6267020
  3. Immunochemical characterization of mammalian protein synthesis initiation factors.
    Biochemistry. 1982 Aug 31;21(18):4206-12 PMID: 6751385
  4. Inhibition of HeLa cell protein synthesis following poliovirus infection correlates with the proteolysis of a 220,000-dalton polypeptide associated with eucaryotic initiation factor 3 and a cap binding protein complex.
    J Biol Chem. 1982 Dec 25;257(24):14806-10 PMID: 6294080
  5. New initiation factor activity required for globin mRNA translation.
    J Biol Chem. 1983 May 10;258(9):5804-10 PMID: 6853548
  6. Demonstration in vitro that eucaryotic initiation factor 3 is active but that a cap-binding protein complex is inactive in poliovirus-infected HeLa cells.
    J Virol. 1984 Sep;51(3):832-7 PMID: 6088805
  7. Assembly of the mitochondrial membrane system. CBP6, a yeast nuclear gene necessary for synthesis of cytochrome b.
    J Biol Chem. 1985 Feb 10;260(3):1513-20 PMID: 2981859
  8. Poliovirus protease does not mediate cleavage of the 220,000-Da component of the cap binding protein complex.
    Proc Natl Acad Sci U S A. 1985 May;82(9):2723-7 PMID: 2986132
  9. Poliovirus protease 3C (P3-7c) does not cleave P220 of the eucaryotic mRNA cap-binding protein complex.
    J Virol. 1985 Aug;55(2):489-93 PMID: 2991572
  10. Eukaryotic protein synthesis.
    Annu Rev Biochem. 1985;54:1109-49 PMID: 3896117
  11. Cleavage of the cap binding protein complex polypeptide p220 is not effected by the second poliovirus protease 2A.
    Virology. 1986 Apr 15;150(1):299-303 PMID: 3006342
  12. A second virus-encoded proteinase involved in proteolytic processing of poliovirus polyprotein.
    Cell. 1986 Jun 6;45(5):761-70 PMID: 3011278
  13. Poliovirus mutant that does not selectively inhibit host cell protein synthesis.
    Mol Cell Biol. 1985 Nov;5(11):2913-23 PMID: 3018486
  14. Initiation of protein synthesis in mammalian cells.
    Biochem J. 1986 May 1;235(3):625-37 PMID: 3530248
  15. Poliovirus polypeptide precursors: expression in vitro and processing by exogenous 3C and 2A proteinases.
    Proc Natl Acad Sci U S A. 1987 Jun;84(12):4002-6 PMID: 3035560
  16. Restriction of translation of capped mRNA in vitro as a model for poliovirus-induced inhibition of host cell protein synthesis: relationship to p220 cleavage.
    J Virol. 1987 Aug;61(8):2480-8 PMID: 3037110
  17. Monoclonal antibody-aided characterization of cellular p220 in uninfected and poliovirus-infected HeLa cells: subcellular distribution and identification of conformers.
    J Virol. 1987 Sep;61(9):2702-10 PMID: 3039164
  18. Poliovirus proteinase 2A induces cleavage of eucaryotic initiation factor 4F polypeptide p220.
    J Virol. 1987 Sep;61(9):2711-8 PMID: 3039165
  19. Impact of virus infection on host cell protein synthesis.
    Annu Rev Biochem. 1987;56:317-32 PMID: 3113326
  20. Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA.
    Nature. 1988 Jul 28;334(6180):320-5 PMID: 2839775
  21. Relationship of p220 cleavage during picornavirus infection to 2A proteinase sequencing.
    J Virol. 1988 Nov;62(11):4216-23 PMID: 2845133
  22. Human immunodeficiency virus tat-activated expression of poliovirus protein 2A inhibits mRNA translation.
    Proc Natl Acad Sci U S A. 1989 Apr;86(7):2143-6 PMID: 2538833
  23. Inhibition of translation in cells infected with a poliovirus 2Apro mutant correlates with phosphorylation of the alpha subunit of eucaryotic initiation factor 2.
    J Virol. 1989 Dec;63(12):5069-75 PMID: 2555543
  24. Poliovirus translation: a paradigm for a novel initiation mechanism.
    Bioessays. 1989 Nov;11(5):128-32 PMID: 2556117
  25. Immunoblot analysis of the structure of protein synthesis initiation factor eIF3 from HeLa cells.
    Arch Biochem Biophys. 1990 Jan;276(1):6-11 PMID: 2297231
  26. Variations in cap-binding complexes from uninfected and poliovirus-infected HeLa cells.
    J Biol Chem. 1990 May 5;265(13):7492-500 PMID: 2159001
  27. 5'-terminal structure of poliovirus polyribosomal RNA is pUp.
    Proc Natl Acad Sci U S A. 1976 Feb;73(2):327-30 PMID: 174102
  28. The 5' end of poliovirus mRNA is not capped with m7G(5')ppp(5')Np.
    Proc Natl Acad Sci U S A. 1976 Feb;73(2):375-80 PMID: 174106
  29. Purification and characterization of initiation factor IF-E3 from rabbit reticulocytes.
    Proc Natl Acad Sci U S A. 1976 Sep;73(9):3005-9 PMID: 1067598
  30. Studies on native ribosomal subunits from rat liver. Purification and characterization of a ribosome dissociation factor.
    Biochemistry. 1977 May 17;16(10):2221-30 PMID: 861207
  31. The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes.
    J Biol Chem. 1978 May 10;253(9):3078-87 PMID: 641056
  32. A polypeptide in eukaryotic initiation factors that crosslinks specifically to the 5'-terminal cap in mRNA.
    Proc Natl Acad Sci U S A. 1978 Oct;75(10):4843-7 PMID: 217002
  33. Protein synthesis initiation factors from rabbit reticulocytes: purification, characterization, and radiochemical labeling.
    Methods Enzymol. 1979;60:15-35 PMID: 459896
  34. Translation of poliovirus RNA in vitro: changes in cleavage pattern and initiation sites by ribosomal salt wash.
    Virology. 1979 Sep;97(2):396-405 PMID: 224589
  35. Purification of a factor that restores translation of vesicular stomatitis virus mRNA in extracts from poliovirus-infected HeLa cells.
    Proc Natl Acad Sci U S A. 1980 Feb;77(2):770-4 PMID: 6244584
  36. The purification and characterization of multiple forms of protein synthesis eukaryotic initiation factors 2, 3, and 5 from rabbit reticulocytes.
    J Biol Chem. 1981 Jan 10;256(1):351-6 PMID: 7451444
  37. Protein synthesis initiation factors from human HeLa cells and rabbit reticulocytes are similar: comparison of protein structure, activities, and immunochemical properties.
    Biochemistry. 1982 Aug 31;21(18):4202-6 PMID: 6181805
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.87.24.9529
Published
1990-12-00
Pages
9529-33
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC55205
Subset
IM
Grants
NIAID NIH HHS · AI-12387 · United States
NIGMS NIH HHS · GM22135 · United States
External Links
PubMed source DOI: 10.1073/pnas.87.24.9529 PMC Full Text View journal details
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