Isolation of human NuMA protein

FEBS Lett. 1994 Nov 14;354(3):307-10. doi: 10.1016/0014-5793(94)01151-6.

Abstract

NuMA is a protein involved in maintenance of nuclear structure and in the assembly of the mitotic spindle. Expression of amino-terminal deletion mutants results in a phenotype identical to that caused by a temperature-sensitive defect of RCC1 (regulator of chromosome condensation). Here we describe the isolation of NuMA protein from HeLa cells under mild conditions as a prerequisite to study its interactions with elements of the RCC1-Ran regulatory pathway. In an overlay assay, NuMA did not bind Ran.[gamma-32P]GTP. Thus it is clearly different from Ran.GTP binding proteins of similar M(r).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigens, Nuclear
  • Cell Cycle Proteins
  • Chromatography, Gel
  • Fluorescent Antibody Technique
  • GTP-Binding Proteins
  • Guanosine Triphosphate / metabolism
  • HeLa Cells / chemistry
  • Humans
  • Immunoblotting
  • Interphase
  • Mitosis
  • Nuclear Matrix-Associated Proteins
  • Nuclear Proteins / isolation & purification*
  • Nuclear Proteins / metabolism
  • Spindle Apparatus*
  • ran GTP-Binding Protein

Substances

  • Antigens, Nuclear
  • Cell Cycle Proteins
  • NUMA1 protein, human
  • Nuclear Matrix-Associated Proteins
  • Nuclear Proteins
  • Guanosine Triphosphate
  • GTP-Binding Proteins
  • ran GTP-Binding Protein