A polyclonal antibody against a fusion protein composed of two vigilin domains and γ-galactosidase was used to localize the tRNA-binding protein vigilin at the ultrastructural level. Immunoreactivity for vigilin was found on membranes bearing ribosomes within the microsome fraction derived from rat livers and on the rough endoplasmic reticulum in rat exocrine pancreatic cells, thus corroborating the involvement of vigilin in protein synthesis. Gold labeling was also found in the nucleus and in the microsome fraction in an osmiophilic substance resembling heterochromatin. Both of these localizations, the rough endoplasmic reticulum and the nucleus, are in line with the observation that a vigilin-containing ribonucleoprotein complex binds tRNA.
Research Areas and Centers
- Academic Focus: Center for Infection and Inflammation Research (ZIEL)