A ribonuclease specific for double-stranded RNA and two distinct ribonuclease H activities from the ribosomal salt wash fraction of Ehrlich ascites tumor cells

Zoya V. Avramova, Zoya I. Galcheva-Gargova

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Abstract

Three distinct nuclease activities, degrading double-stranded substrates, were isolated from the ribosomal salt wash fraction of Ehrlich ascites tumor cells. One of them is an absolutely Mn2+-dependent RNase H, capable of degrading the polyribonucleotide strand of a poly(A) · poly(dT) hybrid only. The other two nuclease activities are: a Mg2+-dependent RNase H and a Mn2+-dependent ribonuclease, specific for double-stranded RNA. These two activities were inseparable by DEAE-cellulose and phosphocellulose chromatography and both were completely inhibited by 20 mmN-ethymaleimide. It is possible that one protein molecule is responsible for the two activities, depending on the nature of the metal ion, though the existence of two different enzyme molecules is not excluded. The three activities are most probably of extranucleolar origin. A function for the double-stranded RNA-specific enzyme is suggested in the processes regulating protein synthesis. The role of the RNase H activities isolated from the ribosomal salt wash fraction is unclear.

Original languageEnglish (US)
Pages (from-to)167-174
Number of pages8
JournalArchives of Biochemistry and Biophysics
Volume204
Issue number1
DOIs
StatePublished - Jan 1 1980

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Ribonuclease H
Ehrlich Tumor Carcinoma
Double-Stranded RNA
Ribonucleases
Tumors
Salts
Cells
Polyribonucleotides
Poly T
DEAE-Cellulose Chromatography
DEAE-Cellulose
Poly A
Molecules
Enzymes
Chromatography
Metal ions
Proteins
Metals
Ions
Substrates

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

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title = "A ribonuclease specific for double-stranded RNA and two distinct ribonuclease H activities from the ribosomal salt wash fraction of Ehrlich ascites tumor cells",
abstract = "Three distinct nuclease activities, degrading double-stranded substrates, were isolated from the ribosomal salt wash fraction of Ehrlich ascites tumor cells. One of them is an absolutely Mn2+-dependent RNase H, capable of degrading the polyribonucleotide strand of a poly(A) · poly(dT) hybrid only. The other two nuclease activities are: a Mg2+-dependent RNase H and a Mn2+-dependent ribonuclease, specific for double-stranded RNA. These two activities were inseparable by DEAE-cellulose and phosphocellulose chromatography and both were completely inhibited by 20 mmN-ethymaleimide. It is possible that one protein molecule is responsible for the two activities, depending on the nature of the metal ion, though the existence of two different enzyme molecules is not excluded. The three activities are most probably of extranucleolar origin. A function for the double-stranded RNA-specific enzyme is suggested in the processes regulating protein synthesis. The role of the RNase H activities isolated from the ribosomal salt wash fraction is unclear.",
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N2 - Three distinct nuclease activities, degrading double-stranded substrates, were isolated from the ribosomal salt wash fraction of Ehrlich ascites tumor cells. One of them is an absolutely Mn2+-dependent RNase H, capable of degrading the polyribonucleotide strand of a poly(A) · poly(dT) hybrid only. The other two nuclease activities are: a Mg2+-dependent RNase H and a Mn2+-dependent ribonuclease, specific for double-stranded RNA. These two activities were inseparable by DEAE-cellulose and phosphocellulose chromatography and both were completely inhibited by 20 mmN-ethymaleimide. It is possible that one protein molecule is responsible for the two activities, depending on the nature of the metal ion, though the existence of two different enzyme molecules is not excluded. The three activities are most probably of extranucleolar origin. A function for the double-stranded RNA-specific enzyme is suggested in the processes regulating protein synthesis. The role of the RNase H activities isolated from the ribosomal salt wash fraction is unclear.

AB - Three distinct nuclease activities, degrading double-stranded substrates, were isolated from the ribosomal salt wash fraction of Ehrlich ascites tumor cells. One of them is an absolutely Mn2+-dependent RNase H, capable of degrading the polyribonucleotide strand of a poly(A) · poly(dT) hybrid only. The other two nuclease activities are: a Mg2+-dependent RNase H and a Mn2+-dependent ribonuclease, specific for double-stranded RNA. These two activities were inseparable by DEAE-cellulose and phosphocellulose chromatography and both were completely inhibited by 20 mmN-ethymaleimide. It is possible that one protein molecule is responsible for the two activities, depending on the nature of the metal ion, though the existence of two different enzyme molecules is not excluded. The three activities are most probably of extranucleolar origin. A function for the double-stranded RNA-specific enzyme is suggested in the processes regulating protein synthesis. The role of the RNase H activities isolated from the ribosomal salt wash fraction is unclear.

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