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. 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).
D000818:Animals; D002467:Cell Nucleus / Q000032:analysis; D002499:Centrifugation, Density Gradient; D055598:Chemical Phenomena; D002621:Chemistry; D003593:Cytoplasm / Q000032:analysis*; D008836:Micrococcal Nuclease; D009698:Nucleoproteins / Q000032:analysis*; D011061:Poly A / Q000032:analysis; D051381:Rats; D012261:Ribonucleoproteins / Q000032:analysis* / Q000302:isolation & purification
D009698:Nucleoproteins; D012261:Ribonucleoproteins; D011061:Poly A; D008836:Micrococcal Nuclease