Yeast RNA polymerase I: A eukaryotic zinc metalloenzyme

David S. Auld, Ikuo Atsuya, Carmen Campino, Pablo Valenzuela

Resultado de la investigación: Article

46 Citas (Scopus)

Resumen

Microwave excitation spectrometry and metal binding inhibition studies show that zinc is a catlytically essential component of the highly purified RNA polymerase I from yeast, the first eukaryotic RNA polymerase I available in quantities sufficient for such studies. It contains 2.4 g-atom of zinc based on a molecular weight of 6.5 × 105 (8). Copper, iron, manganese and magnesium are absent, i.e., below the limits of detection, 10-13 to 10-14 g-atoms. A number of derivatives of 1,10-phenanthroline reversibly inhibit the polymerase catalyzed reaction, apparently by forming a ternary polymerase·Zn·OP complex while the nonchelating isomer, 1,7-phenanthroline, is ineffective.

Idioma originalEnglish
Páginas (desde-hasta)548-554
Número de páginas7
PublicaciónBiochemical and Biophysical Research Communications
Volumen69
N.º2
DOI
EstadoPublished - 22 mar 1976

Huella dactilar

RNA Polymerase I
Yeast
Zinc
Yeasts
Atoms
Manganese
Microwaves
Isomers
Magnesium
Spectrometry
Limit of Detection
Copper
Spectrum Analysis
Iron
Molecular Weight
Metals
Molecular weight
Derivatives
1,10-phenanthroline
1,7-phenanthroline

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Citar esto

Auld, David S. ; Atsuya, Ikuo ; Campino, Carmen ; Valenzuela, Pablo. / Yeast RNA polymerase I : A eukaryotic zinc metalloenzyme. En: Biochemical and Biophysical Research Communications. 1976 ; Vol. 69, N.º 2. pp. 548-554.
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Yeast RNA polymerase I : A eukaryotic zinc metalloenzyme. / Auld, David S.; Atsuya, Ikuo; Campino, Carmen; Valenzuela, Pablo.

En: Biochemical and Biophysical Research Communications, Vol. 69, N.º 2, 22.03.1976, p. 548-554.

Resultado de la investigación: Article

TY - JOUR

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AU - Valenzuela, Pablo

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