Yeast RNA polymerase I: A eukaryotic zinc metalloenzyme

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

doi:10.1016/0006-291X(76)90555-6

Yeast RNA polymerase I: A eukaryotic zinc metalloenzyme

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

Life Sciences School

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2 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 language	English
Pages (from-to)	548-554
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	69
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(76)90555-6
Publication status	Published - 22 Mar 1976

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Yeast RNA polymerase I: A eukaryotic zinc metalloenzyme",

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.",

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T2 - A eukaryotic zinc metalloenzyme

AU - Auld, David S.

AU - Atsuya, Ikuo

AU - Campino, Carmen

AU - Valenzuela, Pablo

PY - 1976/3/22

Y1 - 1976/3/22

N2 - 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.

AB - 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.

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AN - SCOPUS:0017228932

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JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

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ER -

Yeast RNA polymerase I: A eukaryotic zinc metalloenzyme

Abstract

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