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SLBP is associated with histone mRNA on polyribosomes as a component of the histone mRNP

Michael L Whitfield1, Handan Kaygun, Judith A Erkmann

  • 1Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599, USA.

Nucleic Acids Research
|September 11, 2004
PubMed

Insights

Stem-loop binding protein (SLBP) is crucial for histone mRNA processing and translation. In response to DNA replication stress, SLBP relocates to the nucleus, maintaining its RNA binding and processing functions.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Stem-loop binding protein (SLBP) interacts with the 3' end of histone mRNA.
  • SLBP plays roles in both histone pre-mRNA processing and mature mRNA translation.
  • Histone mRNA levels are dynamically regulated by DNA replication and translation inhibitors.

Purpose of the Study:

  • To investigate the role and localization of SLBP in histone mRNA metabolism under different cellular conditions.
  • To determine if SLBP is a component of the histone messenger ribonucleoprotein particle (mRNP).

Main Methods:

  • Immunoprecipitation using anti-SLBP antibodies to isolate histone mRNA-protein complexes.
  • Treatment of cells with inhibitors of DNA replication (e.g., aphidicolin) and translation (e.g., cycloheximide).
  • Analysis of SLBP and histone mRNA localization and activity in response to these treatments.

Main Results:

  • SLBP is confirmed as a component of the histone mRNP.
  • In cycloheximide-treated cells, SLBP is predominantly found on cytoplasmic polyribosomes.
  • Upon inhibition of DNA replication, histone mRNAs degrade, SLBP levels remain stable, and SLBP relocalizes to the nucleus.
  • Nuclear SLBP retains RNA binding and pre-mRNA processing capabilities.

Conclusions:

  • SLBP dynamically regulates its localization between the nucleus and cytoplasm in response to cellular cues.
  • SLBP's nuclear function in histone pre-mRNA processing is maintained even when DNA replication is inhibited.
  • These findings highlight SLBP's critical role in coordinating histone mRNA metabolism with DNA replication status.

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