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. 1972 Nov;69(11):3247–3250. doi: 10.1073/pnas.69.11.3247

A Particle Associated with the Polyadenylate Segment in Mammalian Messenger RNA

Sau-Wah Kwan 1, George Brawerman 1
PMCID: PMC389746  PMID: 4508317

Abstract

A structure consisting of poly(A) complexed with other components is released from polysomes by ribonuclease treatment. The poly(A) complex has a sedimentation value of 12-15, while the corresponding sedimentation value for free poly(A) is 4. The complex does not appear to represent an artifact formed by interaction of free poly(A) with either cytoplasmic or polysomal proteins. The polynucleotide released from the complex by treatment with sodium dodecyl sulfate shows the same electrophoretic mobility as that of poly(A) isolated from deproteinized polysomal RNA. The poly(A) in the complex is partially protected from digestion by T2 ribonuclease. At least part of the poly(A) is available for base pairing with poly(U). The components associated with the poly(A) cause it to bind to Millipore filters at low ionic strength. These components are removed from the complex by Pronase digestion. The findings indicate that the poly(A) segment in messenger RNA serves as a binding site for a particle. This particle appears to consist of proteins.

Keywords: protein-binding site on mRNA, polysome structure

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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