Thermosensitivity of green fluorescent protein fluorescence utilized to reveal novel nuclear-like compartments in a mutant nucleoporin NSP1

J Biochem. 1995 Jul;118(1):13-7. doi: 10.1093/oxfordjournals.jbchem.a124868.


Tagging proteins with the green fluorescent protein (GFP) from Aequorea victoria is a good means of analyzing protein localization in living cells. Nevertheless, GFP and a chimeric protein, GFP-nucleoplasmin, expressed in Saccharomyces cerevisiae were less fluorescent at high culture temperatures. Proteins synthesized at a low temperature retained their fluorescence despite a shift to a higher temperature. Hence, when a temperature-sensitive nsp1 mutant expressing GFP-nucleoplasmin was cultured at 23 degrees C and then shifted to 35 degrees C, we were able to exclusively monitor the localization of the protein synthesized prior to the temperature shift. This protein accumulated in novel nuclear-like compartments devoid of DNA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Calcium-Binding Proteins*
  • Cell Compartmentation
  • Cell Nucleus
  • Fungal Proteins / analysis*
  • Green Fluorescent Proteins
  • Luminescent Proteins / chemistry*
  • Molecular Sequence Data
  • Mutation
  • Nuclear Pore Complex Proteins
  • Nuclear Proteins / analysis*
  • Saccharomyces cerevisiae / chemistry
  • Saccharomyces cerevisiae Proteins*
  • Spectrometry, Fluorescence
  • Temperature*


  • Calcium-Binding Proteins
  • Fungal Proteins
  • Luminescent Proteins
  • NSP1 protein, S cerevisiae
  • Nuclear Pore Complex Proteins
  • Nuclear Proteins
  • Saccharomyces cerevisiae Proteins
  • Green Fluorescent Proteins