Yeast RNA polymerase I: A eukaryotic zinc metalloenzyme

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

Research output: Contribution to journalArticlepeer-review

46 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)548-554
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume69
Issue number2
DOIs
Publication statusPublished - 22 Mar 1976

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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