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Inhibition of nuclear protein import by nonhydrolyzable analogues of GTP and identification of the small GTPase Ran/TC4 as an essential transport factor

Academic Article
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Overview

authors

  • Melchior, F.
  • Paschal, B.
  • Evans, J.
  • Gerace, Larry

publication date

  • December 1993

journal

  • Journal of Cell Biology  Journal

abstract

  • We have investigated a possible involvement of GTPases in nuclear protein import using an in vitro transport system involving digitonin-permeabilized cells supplemented with exogenous cytosol. Transport in this system was measured with a novel ELISA-based assay that allows rapid quantitative analysis. GTP gamma S and other nonhydrolyzable analogues of GTP were found to rapidly inhibit the rate of in vitro nuclear import. Transport inhibition by GTP gamma S was dependent on the concentrations of permeabilized cells and cytosol, and was strongly enhanced by a cytosolic factor(s). The predominant cytosolic component responsible for this inhibition was found in a 20-30-kD fraction in molecular sieving chromatography. Furthermore, a component(s) of this 20-30-kD fraction was itself required for efficient nuclear import. Biochemical complementation with bacterially expressed protein demonstrated that this essential GTP gamma S-sensitive transport factor was Ran/TC4, a previously described GTPase of the Ras superfamily found in both nucleus and cytoplasm. Ran/TC4 and its guanine nucleotide release protein RCC1 have previously been implicated in DNA replication, cell cycle checkpoint control, and RNA synthesis, processing and export. Our results suggest that Ran/TC4 serves to integrate nuclear protein import with these other nuclear activities.

subject areas

  • Amino Acid Sequence
  • Cell Nucleus
  • Cytosol
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme-Linked Immunosorbent Assay
  • GTP Phosphohydrolases
  • GTP-Binding Proteins
  • Guanosine 5'-O-(3-Thiotriphosphate)
  • Guanosine Triphosphate
  • HeLa Cells
  • Humans
  • Kinetics
  • Models, Biological
  • Molecular Sequence Data
  • Molecular Weight
  • Nuclear Proteins
  • Oligopeptides
  • ran GTP-Binding Protein
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Identity

PubMed Central ID

  • PMC2290879

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.123.6.1649

PubMed ID

  • 8276887
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Additional Document Info

start page

  • 1649

end page

  • 1659

volume

  • 123

issue

  • 6

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