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[CBP35-CBP67 interaction in stress response and aging]

H C Schröder1, G Lauc, A P Sève

  • 1Abteilung für Angewandte Molekularbiologie, Universität, Mainz, Germany.

Zeitschrift Fur Gerontologie
|May 1, 1994
PubMed
Summary

Stress causes nuclear CBP35 to bind to glucose-binding CBP67 in mature rats. Old rats do not show this stress response, indicating age-related changes in nuclear protein interactions.

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Area of Science:

  • Molecular biology
  • Cell biology
  • Gerontology

Context:

  • Nuclear ribonucleoprotein (RNP) complexes are vital for RNA processing and transport.
  • Carbohydrate-binding proteins (CBPs) like CBP35 and CBP67 are implicated in nuclear functions.
  • CBP35 has domains suggesting roles in RNP binding and nuclear transport.

Purpose:

  • To investigate the interaction between nuclear CBP35 and CBP67 under stress conditions.
  • To determine if age affects the stress-induced binding of CBP35 to CBP67.

Summary:

  • Stress exposure in mature rats induced binding between nuclear CBP35 and glucose-binding CBP67.
  • This stress-induced interaction was not observed in nuclear extracts from old rats.
  • CBP35 possesses an N-terminal domain similar to heterogeneous nuclear RNP proteins and a C-terminal domain homologous to beta-galactoside-specific lectins.

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Impact:

  • Reveals a novel stress-response mechanism involving CBP35 and CBP67 in mature mammals.
  • Suggests age-related alterations in nuclear protein dynamics and stress response pathways.
  • Provides insights into the molecular mechanisms of nuclear transport and RNP complex regulation.