Literature DB >> 6825854

Efficient translation and polyribosome binding of 125I-labelled rabbit globin messenger ribonucleoprotein.

P D Butcher, H R Arnstein.   

Abstract

Rabbit polyribosomal globin messenger ribonucleoprotein (mRNP) was labelled under mild conditions, using 125I and Iodogen, in the protein moiety so that the fate of mRNA-associated proteins could be followed during translation. 125I-mRNP was shown to retain functional activity in the nuclease-treated reticulocyte lysate translation system under optimal labelling conditions. Polyribsome binding of 125I-mRNP and its sensitivity to cycloheximide indicated a functional- and translation-dependent binding of mRNP proteins. The results constitute a successful and direct approach to the study of mRNA-associated proteins in translational control.

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Year:  1983        PMID: 6825854     DOI: 10.1016/0014-5793(83)80130-6

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


  4 in total

1.  Reconstitution of functional mRNA-protein complexes in a rabbit reticulocyte cell-free translation system.

Authors:  J R Greenberg; E Carroll
Journal:  Mol Cell Biol       Date:  1985-02       Impact factor: 4.272

2.  Physical change in cytoplasmic messenger ribonucleoproteins in cells treated with inhibitors of mRNA transcription.

Authors:  G Dreyfuss; S A Adam; Y D Choi
Journal:  Mol Cell Biol       Date:  1984-03       Impact factor: 4.272

3.  Cross-linking of mRNA to initiation factor eIF-3, 24 kDa cap binding protein and ribosomal proteins S1, S3/3a, S6 and S11 within the 48S pre-initiation complex.

Authors:  P Westermann; O Nygård
Journal:  Nucleic Acids Res       Date:  1984-12-11       Impact factor: 16.971

4.  Interaction of mRNA with proteins in vesicular stomatitis virus-infected cells.

Authors:  S A Adam; Y D Choi; G Dreyfuss
Journal:  J Virol       Date:  1986-02       Impact factor: 5.103

  4 in total

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