Key result
Ultraviolet cross-linking reveals specific proteins bound to polysomal, free, and repressed mRNP.
Why the study?
The specific proteins in direct contact with translationally active and repressed duck globin mRNA were not fully identified.
Answers are grounded in this paper and cite their sources.
A 44 kDa protein specifically interacts with repressed duck globin mRNP particles, while low molecular mass 'prosomal' proteins do not directly interact with the mRNA.
Proteins in direct contact with translationally active and repressed duck globin mRNA were determined by irradiating blood or lysates with ultraviolet light. Cross-linked proteins from polyribosomes and free mRNP particles were 14C-labeled by reductive methylation and identified on SDS-polyacrylamide gels upon autoradiography. Results indicate that ten cross-linked proteins are common to both polysomal and free mRNP, however, a 44 kDa protein appears to be specific for repressed mRNP particles. Furthermore, the notable lack of cross-linked proteins in the 20-30 kDa range in free mRNP supports the view that the characteristic low molecular mass 'prosomal' proteins, previously found associated with translationally repressed duck globin free mRNP [(1984) EMBO J. 3, 29-34], do not interact directly with the mRNA molecule.
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Raymond E. Lockard (1987) studied this question. Ultraviolet light irradiation was evaluated on Proteins in direct contact with translationally active and repressed duck globin mRNA. Ultraviolet cross-linking revealed ten proteins common to polysomal and free mRNP, a 44 kDa protein specific to repressed mRNP, and no direct interaction of 20-30 kDa prosomal proteins with mRNA.
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