Regulation of tyrosine hydroxylase mRNA stability by protein-binding, pyrimidine-rich sequence in the 3'-untranslated region.

doi:10.1074/jbc.274.4.2532

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Article

Regulation of tyrosine hydroxylase mRNA stability by protein-binding, pyrimidine-rich sequence in the 3'-untranslated region.

The Journal of biological chemistry - 22 Jan 1999

Paulding W R, Czyzyk-Krzeska M F

Abstract excerpt

The stability of mRNA for tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine synthesis, is regulated by oxygen tension in the pheochromocytoma-derived PC12 cell line. We previously identified a pyrimidine-rich 27-base-long protein-binding sequence in the 3'-untranslated region o...

Topics

3' Untranslated Regions
Animals
Cell Hypoxia
DNA-Binding Proteins
Enzyme Stability
Hypoxia-Inducible Factor 1
Hypoxia-Inducible Factor 1, alpha Subunit
Molecular Sequence Data
Mutation
Nuclear Proteins
PC12 Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Binding

Pyrimidines

RNA, Messenger

Rats

Transcription Factors

Tyrosine 3-Monooxygenase

Source

Open in PubMed

Identifiers

PMID: 9891025
DOI: 10.1074/jbc.274.4.2532

Genes

PCBP1
PCBP2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9891025-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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