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The protein responsible for the repeating structure of cytoplasmic poly(A)-ribonucleoprotein
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. T...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1983
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2112416/ https://www.ncbi.nlm.nih.gov/pubmed/6833379 |
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collection | PubMed |
description | 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). |
format | Text |
id | pubmed-2112416 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1983 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21124162008-05-01 The protein responsible for the repeating structure of cytoplasmic poly(A)-ribonucleoprotein J Cell Biol Articles 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). The Rockefeller University Press 1983-03-01 /pmc/articles/PMC2112416/ /pubmed/6833379 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles The protein responsible for the repeating structure of cytoplasmic poly(A)-ribonucleoprotein |
title | The protein responsible for the repeating structure of cytoplasmic poly(A)-ribonucleoprotein |
title_full | The protein responsible for the repeating structure of cytoplasmic poly(A)-ribonucleoprotein |
title_fullStr | The protein responsible for the repeating structure of cytoplasmic poly(A)-ribonucleoprotein |
title_full_unstemmed | The protein responsible for the repeating structure of cytoplasmic poly(A)-ribonucleoprotein |
title_short | The protein responsible for the repeating structure of cytoplasmic poly(A)-ribonucleoprotein |
title_sort | protein responsible for the repeating structure of cytoplasmic poly(a)-ribonucleoprotein |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2112416/ https://www.ncbi.nlm.nih.gov/pubmed/6833379 |