The effect of pH on the structure and activity of yeast RNA polymerase I

Paulina Bull, Carmen Campino, Graeme I. Bell, Alejandro Venegas, Pablo Valenzuela

Resultado de la investigación: Article

2 Citas (Scopus)

Resumen

The analysis of the effect of pH upon the rate of polymerization indicates that the activity of yeast RNA polymerase I is optimal between pH 7.5 and 9 and depends on the ionization state of two groups with apparent pKa values of 6.5 and 10. Yeast RNA polymerase I is extremely labile at acid pH. Below pH 5 the enzyme is irreversibly inactivated by [H+], with a second-order rate constant of 1.6 × 10-4 m-1 min-1. Sucrose gradient sedimentation and gel electrophoresis analysis of the enzyme inactivated at acid pH indicates the sequential dissociation of several enzyme subunits. The polypeptides of 44,000 and 24,000 daltons dissociate first from the enzyme core followed by the dissociation of the polypeptides of 48,000 and 36,000 daltons.

Idioma originalEnglish
Páginas (desde-hasta)637-642
Número de páginas6
PublicaciónArchives of Biochemistry and Biophysics
Volumen209
N.º2
DOI
EstadoPublished - 1 ene 1981

Huella dactilar

RNA Polymerase I
Yeast
Yeasts
Enzymes
Acids
Electrophoresis
Sedimentation
Ionization
Sucrose
Rate constants
Polymerization
Gels
Peptides

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

Citar esto

Bull, Paulina ; Campino, Carmen ; Bell, Graeme I. ; Venegas, Alejandro ; Valenzuela, Pablo. / The effect of pH on the structure and activity of yeast RNA polymerase I. En: Archives of Biochemistry and Biophysics. 1981 ; Vol. 209, N.º 2. pp. 637-642.
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The effect of pH on the structure and activity of yeast RNA polymerase I. / Bull, Paulina; Campino, Carmen; Bell, Graeme I.; Venegas, Alejandro; Valenzuela, Pablo.

En: Archives of Biochemistry and Biophysics, Vol. 209, N.º 2, 01.01.1981, p. 637-642.

Resultado de la investigación: Article

TY - JOUR

T1 - The effect of pH on the structure and activity of yeast RNA polymerase I

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AU - Campino, Carmen

AU - Bell, Graeme I.

AU - Venegas, Alejandro

AU - Valenzuela, Pablo

PY - 1981/1/1

Y1 - 1981/1/1

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AB - The analysis of the effect of pH upon the rate of polymerization indicates that the activity of yeast RNA polymerase I is optimal between pH 7.5 and 9 and depends on the ionization state of two groups with apparent pKa values of 6.5 and 10. Yeast RNA polymerase I is extremely labile at acid pH. Below pH 5 the enzyme is irreversibly inactivated by [H+], with a second-order rate constant of 1.6 × 10-4 m-1 min-1. Sucrose gradient sedimentation and gel electrophoresis analysis of the enzyme inactivated at acid pH indicates the sequential dissociation of several enzyme subunits. The polypeptides of 44,000 and 24,000 daltons dissociate first from the enzyme core followed by the dissociation of the polypeptides of 48,000 and 36,000 daltons.

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