Characterization of a ribonuclease from Anacystis nidulans infected with cyanophage as-1

J. Lehmann, W. Völkl, J. Udvardy, G. Borbély, B. Sivók, G. L. Farkas

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

In Anacystis nidulans the ribonuclease (RNase) activity is very low but is greatly increased upon phage-infection. A RNase was isolated and purified over 300-fold from A. nidulans cells infected by cyanophage AS-1. The enzyme did not attack single- or double-stranded DNA, was inactive on p-nitrophenyl phosphate or bis-p-nitrophenyl phosphate as substrates, and had neither 3′- nor 5′-nucleotidase activity. The approximate MW of the enzyme was 12000. Maximal enzyme activity was at pH 7.5. No absolute requirement for metal ions was observed, but Fe3+ stimulated and Co2+ and Ni2+ inhibited enzyme activity. The enzyme is an endonuclease which, upon exhaustive hydrolysis, produces mainly oligonucleotides (average chain-length: 3) with 3′-P termini. Analysis of the base composition of these oligonucleotides and determination of their 3′-terminal nucleosides, together with the investigation of the rate of hydrolysis of synthetic polyribonucleotides, have shown that the enzyme has a relative specificity for uridylic acid.

Original languageEnglish
Pages (from-to)541-544
Number of pages4
JournalPhytochemistry
Volume18
Issue number4
DOIs
Publication statusPublished - 1979

Fingerprint

ribonucleases
Ribonucleases
Enzyme activity
Enzymes
enzymes
oligonucleotides
Oligonucleotides
Hydrolysis
hydrolysis
Polyribonucleotides
phosphates
enzyme activity
5'-nucleotidase
Uridine Monophosphate
5'-Nucleotidase
Bacteriophages
nucleosides
Endonucleases
Single-Stranded DNA
metal ions

Keywords

  • Anacystis nidulans
  • blue-green alga
  • cyanophage infection
  • Cyanophyceae
  • phylogenetics.
  • ribonuclease

ASJC Scopus subject areas

  • Plant Science
  • Biochemistry
  • Molecular Biology
  • Organic Chemistry
  • Drug Discovery

Cite this

Characterization of a ribonuclease from Anacystis nidulans infected with cyanophage as-1. / Lehmann, J.; Völkl, W.; Udvardy, J.; Borbély, G.; Sivók, B.; Farkas, G. L.

In: Phytochemistry, Vol. 18, No. 4, 1979, p. 541-544.

Research output: Contribution to journalArticle

Lehmann, J. ; Völkl, W. ; Udvardy, J. ; Borbély, G. ; Sivók, B. ; Farkas, G. L. / Characterization of a ribonuclease from Anacystis nidulans infected with cyanophage as-1. In: Phytochemistry. 1979 ; Vol. 18, No. 4. pp. 541-544.
@article{671363a1017d4f3ebd0ad4da7b4926d3,
title = "Characterization of a ribonuclease from Anacystis nidulans infected with cyanophage as-1",
abstract = "In Anacystis nidulans the ribonuclease (RNase) activity is very low but is greatly increased upon phage-infection. A RNase was isolated and purified over 300-fold from A. nidulans cells infected by cyanophage AS-1. The enzyme did not attack single- or double-stranded DNA, was inactive on p-nitrophenyl phosphate or bis-p-nitrophenyl phosphate as substrates, and had neither 3′- nor 5′-nucleotidase activity. The approximate MW of the enzyme was 12000. Maximal enzyme activity was at pH 7.5. No absolute requirement for metal ions was observed, but Fe3+ stimulated and Co2+ and Ni2+ inhibited enzyme activity. The enzyme is an endonuclease which, upon exhaustive hydrolysis, produces mainly oligonucleotides (average chain-length: 3) with 3′-P termini. Analysis of the base composition of these oligonucleotides and determination of their 3′-terminal nucleosides, together with the investigation of the rate of hydrolysis of synthetic polyribonucleotides, have shown that the enzyme has a relative specificity for uridylic acid.",
keywords = "Anacystis nidulans, blue-green alga, cyanophage infection, Cyanophyceae, phylogenetics., ribonuclease",
author = "J. Lehmann and W. V{\"o}lkl and J. Udvardy and G. Borb{\'e}ly and B. Siv{\'o}k and Farkas, {G. L.}",
year = "1979",
doi = "10.1016/S0031-9422(00)84256-9",
language = "English",
volume = "18",
pages = "541--544",
journal = "Phytochemistry",
issn = "0031-9422",
publisher = "Elsevier Limited",
number = "4",

}

TY - JOUR

T1 - Characterization of a ribonuclease from Anacystis nidulans infected with cyanophage as-1

AU - Lehmann, J.

AU - Völkl, W.

AU - Udvardy, J.

AU - Borbély, G.

AU - Sivók, B.

AU - Farkas, G. L.

PY - 1979

Y1 - 1979

N2 - In Anacystis nidulans the ribonuclease (RNase) activity is very low but is greatly increased upon phage-infection. A RNase was isolated and purified over 300-fold from A. nidulans cells infected by cyanophage AS-1. The enzyme did not attack single- or double-stranded DNA, was inactive on p-nitrophenyl phosphate or bis-p-nitrophenyl phosphate as substrates, and had neither 3′- nor 5′-nucleotidase activity. The approximate MW of the enzyme was 12000. Maximal enzyme activity was at pH 7.5. No absolute requirement for metal ions was observed, but Fe3+ stimulated and Co2+ and Ni2+ inhibited enzyme activity. The enzyme is an endonuclease which, upon exhaustive hydrolysis, produces mainly oligonucleotides (average chain-length: 3) with 3′-P termini. Analysis of the base composition of these oligonucleotides and determination of their 3′-terminal nucleosides, together with the investigation of the rate of hydrolysis of synthetic polyribonucleotides, have shown that the enzyme has a relative specificity for uridylic acid.

AB - In Anacystis nidulans the ribonuclease (RNase) activity is very low but is greatly increased upon phage-infection. A RNase was isolated and purified over 300-fold from A. nidulans cells infected by cyanophage AS-1. The enzyme did not attack single- or double-stranded DNA, was inactive on p-nitrophenyl phosphate or bis-p-nitrophenyl phosphate as substrates, and had neither 3′- nor 5′-nucleotidase activity. The approximate MW of the enzyme was 12000. Maximal enzyme activity was at pH 7.5. No absolute requirement for metal ions was observed, but Fe3+ stimulated and Co2+ and Ni2+ inhibited enzyme activity. The enzyme is an endonuclease which, upon exhaustive hydrolysis, produces mainly oligonucleotides (average chain-length: 3) with 3′-P termini. Analysis of the base composition of these oligonucleotides and determination of their 3′-terminal nucleosides, together with the investigation of the rate of hydrolysis of synthetic polyribonucleotides, have shown that the enzyme has a relative specificity for uridylic acid.

KW - Anacystis nidulans

KW - blue-green alga

KW - cyanophage infection

KW - Cyanophyceae

KW - phylogenetics.

KW - ribonuclease

UR - http://www.scopus.com/inward/record.url?scp=49249150720&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=49249150720&partnerID=8YFLogxK

U2 - 10.1016/S0031-9422(00)84256-9

DO - 10.1016/S0031-9422(00)84256-9

M3 - Article

AN - SCOPUS:49249150720

VL - 18

SP - 541

EP - 544

JO - Phytochemistry

JF - Phytochemistry

SN - 0031-9422

IS - 4

ER -