Abstract
A 75,000-dalton protein has been purified approximately 1,000-fold from rat liver, based on its capacity to organize poly(A) in a 27-residue repeating structure. This protein may be identified with the major polypeptide component of cytoplasmic poly(A)-ribonucleoprotein (RNP) previously described. The poly(A)-organizing activity of the protein is detected only in cytoplasmic fractions. Upon nuclease digestion of the 75,000-dalton protein-poly(A) complex, monomers, and higher multimers of RNP subunits can be resolved in a sucrose gradient. The sedimentation rate of the monomer is compatible with a composition of one 75,000-dalton protein molecule and one 27-residue segment of poly(A).
Dates
Type | When |
---|---|
Created | 21 years, 3 months ago (May 14, 2004, 7:04 p.m.) |
Deposited | 2 years, 1 month ago (July 24, 2023, 2:37 p.m.) |
Indexed | 1 month ago (July 20, 2025, 12:17 a.m.) |
Issued | 42 years, 5 months ago (March 1, 1983) |
Published | 42 years, 5 months ago (March 1, 1983) |
Published Online | 42 years, 5 months ago (March 1, 1983) |
Published Print | 42 years, 5 months ago (March 1, 1983) |
@article{Baer_1983, title={The protein responsible for the repeating structure of cytoplasmic poly(A)-ribonucleoprotein.}, volume={96}, ISSN={1540-8140}, url={http://dx.doi.org/10.1083/jcb.96.3.717}, DOI={10.1083/jcb.96.3.717}, number={3}, journal={The Journal of cell biology}, publisher={Rockefeller University Press}, author={Baer, B W and Kornberg, R D}, year={1983}, month=mar, pages={717–721} }