Presence of elongation factor 1 in nuclei and nucleoli of rat liver

Cell Biol Int Rep. 1978 Jan;2(1):25-32. doi: 10.1016/0309-1651(78)90081-4.


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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cell Nucleolus / analysis*
  • Cell Nucleus / analysis*
  • Cell Nucleus / enzymology
  • Cell-Free System
  • L-Lactate Dehydrogenase / metabolism
  • Liver / ultrastructure
  • Male
  • Peptide Elongation Factors / analysis*
  • Protein Binding
  • Protein Biosynthesis
  • RNA, Transfer / metabolism
  • Rats
  • Ribosomes / metabolism


  • Peptide Elongation Factors
  • RNA, Transfer
  • L-Lactate Dehydrogenase