Study of localization of the protein-synthesizing machinery along actin filament bundles

Cell Biol Int. 1993 Apr;17(4):409-16. doi: 10.1006/cbir.1993.1079.

Abstract

Indirect immunofluorescent microscopy was used to study the distribution of elongation factor 2 (eEF-2) in fixed human skin diploid and mouse embryo fibroblasts. It was found earlier that some of the eEF-2, ribosomes and initiation factor 2 (eIF-2) are co-localized with a part of the actin microfilament bundles in these cells (Gavrilova et al., 1987; Shestakova et al., 1991). Here it has been shown that inhibition of protein synthesis either by inactivation of eEF-2 itself with diphtheria toxin or by inactivation of ribosomes with ricin does not abolish the distribution of eEF-2 along the actin microfilament bundles. At the same time, the disassembly of actin microfilaments by cytochalasin D results also in the disappearance of eEF-2- carrying threads. This means that the eEF-2-carrying threads do not exist per se, and that the organization of eEF-2 in visible "filaments" depends upon the integrity of the actin cytoskeleton.

MeSH terms

  • Actin Cytoskeleton / drug effects
  • Actin Cytoskeleton / metabolism*
  • Actins / physiology*
  • Animals
  • Cells, Cultured
  • Cytochalasin D / pharmacology
  • Diphtheria Toxin / pharmacology
  • Embryo, Mammalian
  • Eukaryotic Initiation Factor-2 / metabolism*
  • Fibroblasts / cytology
  • Fibroblasts / drug effects
  • Fibroblasts / metabolism
  • Humans
  • Leucine / metabolism
  • Mice
  • Peptide Elongation Factor 2
  • Peptide Elongation Factors / metabolism*
  • Protein Biosynthesis*
  • Ribosomes / metabolism
  • Skin / cytology
  • Skin / metabolism*

Substances

  • Actins
  • Diphtheria Toxin
  • Eukaryotic Initiation Factor-2
  • Peptide Elongation Factor 2
  • Peptide Elongation Factors
  • Cytochalasin D
  • Leucine