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Related Experiment Videos

Changes in heterogeneous nuclear RNP core polypeptide complements during the cell cycle.

G P Leser1, T E Martin

  • 1Department of Molecular Genetics and Cell Biology, University of Chicago, Illinois 60637.

The Journal of Cell Biology
|November 1, 1987
PubMed
Summary

Mammalian heterogeneous nuclear ribonucleoprotein (hnRNP) core proteins shift during cell division. These core hnRNP proteins, normally nuclear, relocate to the cytoplasm during mitosis, with altered forms appearing.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Mammalian heterogeneous nuclear ribonucleoprotein (hnRNP) complexes are crucial for RNA processing and transport.
  • These complexes consist of core polypeptides (chrp) that are typically localized to the nucleus.

Purpose of the Study:

  • To investigate the cell cycle-dependent changes in the composition and localization of hnRNP core proteins.
  • To characterize the modifications and distribution of hnRNP proteins during mitosis.

Main Methods:

  • Synchronized HeLa cell populations were analyzed across different cell cycle stages (S, G2, mitosis, G1).
  • Two-dimensional immunoblot analysis was used to examine hnRNP core protein complements.
  • Sucrose density gradient centrifugation and RNase digestion were employed to study cytoplasmic hnRNP complexes.

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Main Results:

  • The complement of hnRNP core proteins changes during mitosis, with specific polypeptides appearing or diminishing.
  • Mitosis-specific modified forms of hnRNP proteins were detected in the cytoplasmic fraction.
  • These modified cytoplasmic hnRNP complexes exhibit sedimentation properties similar to nuclear hnRNP complexes.

Conclusions:

  • hnRNP core proteins undergo physiological modifications and redistribution during the cell cycle, particularly during mitosis.
  • Mitosis-specific hnRNP forms are found in the cytoplasm, suggesting a role in cell division.
  • The fundamental structure of RNA/protein complexes in mitotic cytoplasm resembles that of nuclear hnRNP.