Presence of elongation factor 1 in nuclei and nucleoli of rat liver.
Purified rat liver nuclei contain 11% of the total cellular translation elongation factor 1 activity. Ninety percent of the nuclear EF-1 activity was in the nucleoplasm and 10% was nucleolar. The specific activities of the nuclear and nucleolar EF-1 were 2 to 3 times higher, respectively, than EF-1 activity of the liver homogenate. The presence of EF-1 in the purified nuclei did not result from cytoplasmic contamination since only 0.14% of the cellular lactate dehydrogenase was present in the nuclei. These results provide the first evidence for the presence in the cell nucleus of translational factors of protein synthesis.
D000818:Animals; D002466:Cell Nucleolus / Q000032:analysis*; D002467:Cell Nucleus / Q000032:analysis* / Q000201:enzymology; D002474:Cell-Free System; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D008099:Liver / Q000648:ultrastructure; D008297:Male; D010445:Peptide Elongation Factors / Q000032:analysis*; D011485:Protein Binding; D014176:Protein Biosynthesis; D012343:RNA, Transfer / Q000378:metabolism; D051381:Rats; D012270:Ribosomes / Q000378:metabolism
D010445:Peptide Elongation Factors; D012343:RNA, Transfer; D007770:L-Lactate Dehydrogenase