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Is human histone gene expression autogenously regulated?

G S Stein, J L Stein

Molecular and Cellular Biochemistry

|September 1, 1984

Summary

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Histone mRNA levels rise with DNA synthesis, but their stability is controlled post-transcriptionally. Termination of DNA replication triggers histone mRNA degradation via unbound histones affecting translation complexes.

Area of Science:

Molecular Biology
Cell Biology
Biochemistry

Background:

Core and H1 histone messenger RNAs (mRNAs) increase during DNA synthesis, indicating transcriptional control of histone gene expression early in S phase.
Histone protein synthesis throughout S phase is regulated by the availability of histone mRNAs.
Histone mRNA stability and destabilization upon completion or inhibition of DNA replication are selective, tightly coupled, and primarily post-transcriptionally controlled.

Purpose of the Study:

To propose a model explaining the post-transcriptional regulation of histone mRNA turnover.
To elucidate the mechanism by which histone mRNA destabilization occurs after DNA replication termination.

Main Methods:

The study presents a theoretical model based on existing experimental observations.

Related Experiment Videos

The model focuses on the interplay between newly synthesized histone proteins, histone mRNAs, and cellular ribonucleases.

Main Results:

Termination of DNA replication leads to a loss of binding sites for newly synthesized histones, causing their transient accumulation.
Unbound histones interact with the histone translation complex on polysomal histone mRNAs.
This interaction renders histone mRNAs susceptible to degradation by cellular ribonucleases.

Conclusions:

The proposed model explains the rapid, RNA synthesis-independent destabilization of histone mRNAs following DNA replication inhibition.
The mechanism highlights the crucial role of post-transcriptional control in regulating histone mRNA turnover.
Protein synthesis is required for the initiation of histone mRNA destabilization, as proposed by the model.