Possible involvement of messenger RNA-associated proteins in protein synthesis.
Two distinct forms of globin messenger RNA were isolated from mouse spleen cells infected with Friend erythroleukemia virus: polyribosomal messenger ribonucleoprotein particles (15S mRNP), and their corresponding protein-free mRNAs obtained by chemical deproteinization. The translation efficiencies of both messenger forms were assayed in a Krebs II ascites cell-free system. Selective removal of RNA-binding proteins from the ascites cell lysate did not affect globin synthesis when the mRNA was supplied as 15S mRNP; deproteinized mRNA however was not translated. Only in the presence of two fractions of RNA-binding proteins was the protein-free mRNA translated. Some of the RNA-binding proteins have the same molecular weights and isoelectric points as the principal proteins of 15S mRNP.
D000818:Animals; D002352:Carrier Proteins / Q000502:physiology*; D002458:Cell Fractionation; D002474:Cell-Free System; D005622:Friend murine leukemia virus; D005914:Globins / Q000096:biosynthesis* / Q000235:genetics; D007942:Leukemia, Experimental / Q000235:genetics; D051379:Mice; D008807:Mice, Inbred BALB C; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000502:physiology*; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins / Q000032:analysis; D013154:Spleen / Q000378:metabolism
D002352:Carrier Proteins; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins; C026452:messenger ribonucleoprotein; D005914:Globins