Identification of a nuclear protein binding element within the rat brain protein kinase C γ promoter that is related to the developmental control of this gene

Kuang Hua Chen, Steven Widen, Samuel H. Wilson, Kuo Ping Huang

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Protein kinase C γ (PKC γ) is a brain-specific isozyme expressed at a high level in the adult but not in the fetal or newborn rat. At least seventeen nuclear protein binding sites within the 5'-flanking region extending from -1612 to +243 had been identified by DNase I footprinting analysis and gel mobility shift assays. Among them, one site, GAATTAATAGG, at -669 to -679 is protected from DNase I digestion by nuclear protein from newborn but not from the adult rat brain. The levels of this binding protein, as determined by gel mobility shift assay, were found inversely related to the levels of PKC γ in rat brain at different stages of development. These results suggest that this particular binding site may participate in the developmental regulation of PKC γ gene.

Original languageEnglish (US)
Pages (from-to)210-214
Number of pages5
JournalFEBS Letters
Volume325
Issue number3
DOIs
StatePublished - Jul 5 1993
Externally publishedYes

Fingerprint

Developmental Genes
Nuclear Proteins
Protein Binding
Protein Kinase C
Rats
Brain
Genes
Deoxyribonuclease I
Electrophoretic Mobility Shift Assay
Assays
Gels
Binding Sites
5' Flanking Region
Isoenzymes
Digestion
Carrier Proteins

Keywords

  • Developmental regulation
  • DNA binding protein
  • Protein kinase C γ gene

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Identification of a nuclear protein binding element within the rat brain protein kinase C γ promoter that is related to the developmental control of this gene. / Chen, Kuang Hua; Widen, Steven; Wilson, Samuel H.; Huang, Kuo Ping.

In: FEBS Letters, Vol. 325, No. 3, 05.07.1993, p. 210-214.

Research output: Contribution to journalArticle

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