Are all nucleotidyl transferases metalloenzymes?

Pablo Valenzuela, Robert W. Morris, Anthony Faras, Warren Levinson, William J. Rutter

Resultado de la investigación: Article

61 Citas (Scopus)

Resumen

Previous studies (1,2) have shown that DNA polymerases (sea urchin and E. coli I) and E. coli RNA polymerases are zinc metalloproteins. We report here that DNA-dependent RNA polymerases I and II from rat liver, I, II and III from sea urchin, and RNA-dependent DNA polymerase (reverse transcriptase) from Rous sarcoma virus are inhibited by pre-incubation with the chelating agent, o-phenanthroline. These enzymes are not affected by pre-incubation with the related compound, m-phenanthroline, which is not a metal chelating agent. The data suggest that, in addition to Mg++ or Mn++, the enzymes require a tightly bound metal ion (possibly zinc) for catalytic activity. The DNA-terminal transferase is also inhibited by o-phenanthroline but not m-phenanthroline (3). On the other hand, we found that tRNA-nucleotidyl transferases from Rous sarcoma virions and yeast are not affected by either o- or m-phenanthroline. These observations suggest that many but not all nucleotidyl transferases are metallo-enzymes.

Idioma originalEnglish
Páginas (desde-hasta)1036-1041
Número de páginas6
PublicaciónBiochemical and Biophysical Research Communications
Volumen53
N.º3
DOI
EstadoPublished - 6 ago 1973

Huella dactilar

Phenanthrolines
Transferases
Sea Urchins
RNA-Directed DNA Polymerase
Chelating Agents
Escherichia coli
Zinc
Enzymes
Avian Sarcoma
Metalloproteins
RNA Polymerase I
Rous sarcoma virus
RNA Polymerase II
DNA-Directed DNA Polymerase
DNA-Directed RNA Polymerases
Transfer RNA
Viruses
Virion
Liver
Yeast

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Cell Biology

Citar esto

Valenzuela, P., Morris, R. W., Faras, A., Levinson, W., & Rutter, W. J. (1973). Are all nucleotidyl transferases metalloenzymes? Biochemical and Biophysical Research Communications, 53(3), 1036-1041. https://doi.org/10.1016/0006-291X(73)90196-4
Valenzuela, Pablo ; Morris, Robert W. ; Faras, Anthony ; Levinson, Warren ; Rutter, William J. / Are all nucleotidyl transferases metalloenzymes?. En: Biochemical and Biophysical Research Communications. 1973 ; Vol. 53, N.º 3. pp. 1036-1041.
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Valenzuela, P, Morris, RW, Faras, A, Levinson, W & Rutter, WJ 1973, 'Are all nucleotidyl transferases metalloenzymes?', Biochemical and Biophysical Research Communications, vol. 53, n.º 3, pp. 1036-1041. https://doi.org/10.1016/0006-291X(73)90196-4

Are all nucleotidyl transferases metalloenzymes? / Valenzuela, Pablo; Morris, Robert W.; Faras, Anthony; Levinson, Warren; Rutter, William J.

En: Biochemical and Biophysical Research Communications, Vol. 53, N.º 3, 06.08.1973, p. 1036-1041.

Resultado de la investigación: Article

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AU - Morris, Robert W.

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AU - Levinson, Warren

AU - Rutter, William J.

PY - 1973/8/6

Y1 - 1973/8/6

N2 - Previous studies (1,2) have shown that DNA polymerases (sea urchin and E. coli I) and E. coli RNA polymerases are zinc metalloproteins. We report here that DNA-dependent RNA polymerases I and II from rat liver, I, II and III from sea urchin, and RNA-dependent DNA polymerase (reverse transcriptase) from Rous sarcoma virus are inhibited by pre-incubation with the chelating agent, o-phenanthroline. These enzymes are not affected by pre-incubation with the related compound, m-phenanthroline, which is not a metal chelating agent. The data suggest that, in addition to Mg++ or Mn++, the enzymes require a tightly bound metal ion (possibly zinc) for catalytic activity. The DNA-terminal transferase is also inhibited by o-phenanthroline but not m-phenanthroline (3). On the other hand, we found that tRNA-nucleotidyl transferases from Rous sarcoma virions and yeast are not affected by either o- or m-phenanthroline. These observations suggest that many but not all nucleotidyl transferases are metallo-enzymes.

AB - Previous studies (1,2) have shown that DNA polymerases (sea urchin and E. coli I) and E. coli RNA polymerases are zinc metalloproteins. We report here that DNA-dependent RNA polymerases I and II from rat liver, I, II and III from sea urchin, and RNA-dependent DNA polymerase (reverse transcriptase) from Rous sarcoma virus are inhibited by pre-incubation with the chelating agent, o-phenanthroline. These enzymes are not affected by pre-incubation with the related compound, m-phenanthroline, which is not a metal chelating agent. The data suggest that, in addition to Mg++ or Mn++, the enzymes require a tightly bound metal ion (possibly zinc) for catalytic activity. The DNA-terminal transferase is also inhibited by o-phenanthroline but not m-phenanthroline (3). On the other hand, we found that tRNA-nucleotidyl transferases from Rous sarcoma virions and yeast are not affected by either o- or m-phenanthroline. These observations suggest that many but not all nucleotidyl transferases are metallo-enzymes.

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