A third DNA-dependent ATPase from Bacillus cereus free of ATP-dependent DNase activity

A. Ohlbaum, S. Csuzi, F. Antoni, G. Bánfalvi

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

The purification of ATP-dependent DNase from Bacillus cereus led to the isolation and characterization of a third DNA-dependent ATPase. The enzyme called ATPase III has been purified free of nuclease activity. None of the expected ATPases proved to be identical with ATP-dependent DNase-DNA-dependent ATPase. Separation of ATPase I, II and III and a DNase specific for single-stranded DNA from the same source excludes the possibility of ATP-dependent DNase being the action of a single enzyme molecule.

Original languageEnglish
Pages (from-to)63-67
Number of pages5
JournalFEBS Letters
Volume158
Issue number1
DOIs
Publication statusPublished - Jul 11 1983

Fingerprint

Exodeoxyribonuclease V
Bacillus cereus
Adenosine Triphosphatases
Deoxyribonucleases
Single-Stranded DNA
Enzymes
Purification
Molecules

Keywords

  • ATP dependence
  • ATPase
  • DNA dependence
  • DNase
  • Recombination
  • Unwinding

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

A third DNA-dependent ATPase from Bacillus cereus free of ATP-dependent DNase activity. / Ohlbaum, A.; Csuzi, S.; Antoni, F.; Bánfalvi, G.

In: FEBS Letters, Vol. 158, No. 1, 11.07.1983, p. 63-67.

Research output: Contribution to journalArticle

Ohlbaum, A. ; Csuzi, S. ; Antoni, F. ; Bánfalvi, G. / A third DNA-dependent ATPase from Bacillus cereus free of ATP-dependent DNase activity. In: FEBS Letters. 1983 ; Vol. 158, No. 1. pp. 63-67.
@article{18f545a9064b499a8de1a5cb1cea3f53,
title = "A third DNA-dependent ATPase from Bacillus cereus free of ATP-dependent DNase activity",
abstract = "The purification of ATP-dependent DNase from Bacillus cereus led to the isolation and characterization of a third DNA-dependent ATPase. The enzyme called ATPase III has been purified free of nuclease activity. None of the expected ATPases proved to be identical with ATP-dependent DNase-DNA-dependent ATPase. Separation of ATPase I, II and III and a DNase specific for single-stranded DNA from the same source excludes the possibility of ATP-dependent DNase being the action of a single enzyme molecule.",
keywords = "ATP dependence, ATPase, DNA dependence, DNase, Recombination, Unwinding",
author = "A. Ohlbaum and S. Csuzi and F. Antoni and G. B{\'a}nfalvi",
year = "1983",
month = "7",
day = "11",
doi = "10.1016/0014-5793(83)80677-2",
language = "English",
volume = "158",
pages = "63--67",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - A third DNA-dependent ATPase from Bacillus cereus free of ATP-dependent DNase activity

AU - Ohlbaum, A.

AU - Csuzi, S.

AU - Antoni, F.

AU - Bánfalvi, G.

PY - 1983/7/11

Y1 - 1983/7/11

N2 - The purification of ATP-dependent DNase from Bacillus cereus led to the isolation and characterization of a third DNA-dependent ATPase. The enzyme called ATPase III has been purified free of nuclease activity. None of the expected ATPases proved to be identical with ATP-dependent DNase-DNA-dependent ATPase. Separation of ATPase I, II and III and a DNase specific for single-stranded DNA from the same source excludes the possibility of ATP-dependent DNase being the action of a single enzyme molecule.

AB - The purification of ATP-dependent DNase from Bacillus cereus led to the isolation and characterization of a third DNA-dependent ATPase. The enzyme called ATPase III has been purified free of nuclease activity. None of the expected ATPases proved to be identical with ATP-dependent DNase-DNA-dependent ATPase. Separation of ATPase I, II and III and a DNase specific for single-stranded DNA from the same source excludes the possibility of ATP-dependent DNase being the action of a single enzyme molecule.

KW - ATP dependence

KW - ATPase

KW - DNA dependence

KW - DNase

KW - Recombination

KW - Unwinding

UR - http://www.scopus.com/inward/record.url?scp=0021101083&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021101083&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(83)80677-2

DO - 10.1016/0014-5793(83)80677-2

M3 - Article

C2 - 6134644

AN - SCOPUS:0021101083

VL - 158

SP - 63

EP - 67

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1

ER -