Association of cap binding protein‐related polypeptides with cytoplasmic RNP particles of chick embryonic muscle

Chakraborty, Dipak; Mukherjee, Asok K.; Sarkar, Satyapriya; Lee, Kevin A.W.; Darveau, André; Sonenberg, Nahum

doi:10.1016/0014-5793(82)81064-8

Cited by 6 publications

References 24 publications

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Stoichiometric association of cap-binding protein I with translated polysomal globin mRNP.

Görlach¹,

Hilse²

1986

The EMBO Journal

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The protein composition of a 12S polysomal globin messenger ribonucleoprotein (pmRNP) from rabbit reticulocytes was examined. The pmRNP was released from purified polysomes by puromycin treatment under run‐off conditions of protein synthesis. The protein pattern of this pmRNP depends on the potassium ion concentration used during the run‐off and the subsequent isolation. Several proteins show a salt‐dependent association with the pmRNP while a few are constituents of the pmRNP at all salt concentrations tested. By cross‐linking the pmRNP‐derived proteins to [3H]methyl‐labelled oxidized vesicular stomatitis virus (VSV) mRNA and by immunoblotting against anti‐cap‐binding protein (CBP I) antibodies, it is demonstrated that the association of the CBP I with the pmRNP depends on the ionic strength. At 65 mM KCl, CBP I shows low affinity for the pmRNP; at 140 mM KCl, the affinity of CBP I for the pmRNP is greatly enhanced. At this ionic strength, equimolar amounts of CBP I and mRNA are found in the pmRNP. At 500 mM KCl, the pmRNP is completely devoid of CBP I. In the non‐translated free cytoplasmic mRNP (cmRNP) no CBP can be detected by either the cross‐link or the immunoblot technique.

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Stoichiometric association of cap-binding protein I with translated polysomal globin mRNP.

Görlach¹,

Hilse²

1986

The EMBO Journal

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Nucleo-Cytoplasmic Transport of mRNA: Its Relationship to RNA Metabolism, Subcellular Structures and Other Nucleocytoplasmic Exchanges

Agutter

1988

Progress in Molecular and Subcellular Biology

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The function of proteins that interact with mRNA

Larson

Sells

1987

Mol Cell Biochem

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Specific proteins are associated with mRNA in the cytoplasm of eukaryotic cells. The complement of associated proteins depends upon whether the mRNA is an integral component of the polysomal complex being translated, or, alternatively, whether it is part of the non-translated free mRNP fraction. By subjecting cells to ultraviolet irradiation in vivo to cross-link proteins to mRNA, mRNP proteins have been shown to be associated with specific regions of the mRNA molecule. Examination of mRNP complexes containing a unique mRNA has suggested that not all mRNA contain the same family of associated RNA binding proteins. The functions of mRNA associated proteins may include a role in providing stability for mRNA, and/or in modulating translation. With the recent demonstrations that both free and polysomal mRNPs are associated with the cytoskeletal framework, specific mRNP proteins may play a role in determining the subcellular localization of specific mRNPs.

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Association of cap binding protein‐related polypeptides with cytoplasmic RNP particles of chick embryonic muscle

Cited by 6 publications

References 24 publications

Stoichiometric association of cap-binding protein I with translated polysomal globin mRNP.

Stoichiometric association of cap-binding protein I with translated polysomal globin mRNP.

Nucleo-Cytoplasmic Transport of mRNA: Its Relationship to RNA Metabolism, Subcellular Structures and Other Nucleocytoplasmic Exchanges

The function of proteins that interact with mRNA

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