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HuR stabilizes a polyadenylated form of replication-dependent histone mRNAs under stress conditions

Incheol Ryu1,2, Yeonkyoung Park1,2, Jwa-Won Seo3

  • 1Creative Research Initiatives Center for Molecular Biology of Translation, Korea University, Seoul, South Korea.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|October 11, 2018
PubMed

Insights

Stress stabilizes a polyadenylated form of replication-dependent histone (RDH) mRNAs. The human antigen R (HuR) protein binds the 3' untranslated region, regulating expression independently of translation.

Area of Science:

  • Molecular Biology
  • Gene Regulation
  • RNA Biology

Background:

  • Metazoan mRNAs typically possess a 3' poly(A) tail, except for replication-dependent histone (RDH) mRNAs, which feature a stem-loop (SL) structure.
  • A small fraction of RDH mRNAs are polyadenylated under physiological conditions, but the mechanisms remain unclear.

Purpose of the Study:

  • To investigate the molecular mechanisms governing the biogenesis of polyadenylated RDH [poly(A)+ RDH] mRNAs.
  • To identify factors and conditions that influence the stability and expression of poly(A)+ RDH mRNAs.

Main Methods:

  • Genome-wide analyses of mRNA stability under stress conditions (puromycin treatment, UVC irradiation).
  • Investigation of translation-independent mechanisms.
  • Assessment of human antigen R (HuR) binding to the 3' untranslated region (UTR) of RDH mRNAs.

Main Results:

  • Puromycin treatment and UVC irradiation stabilize poly(A)+ RDH mRNAs relative to canonical SL-ending RDH mRNAs.
  • Stabilization of poly(A)+ RDH mRNAs is translation-independent.
  • HuR binding to the extended 3' UTR is crucial for regulating poly(A)+ RDH mRNA stability under stress.

Conclusions:

  • HuR plays a significant role in regulating the expression of polyadenylated RDH mRNAs.
  • Stress conditions can alter RDH mRNA processing, leading to a polyadenylated form regulated by HuR.
Keywords:
3′UTRUVCmRNA stabilitypolyadenylation signal

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