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PMID: 6275125 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Properties of an intracisternal A-particle-associated endonuclease activity which is stimulated by ATP.

Journal of virology ·Vol. 40 ·No. 3 ·1981-12-00 ·Pages 927-31

Nissen-Meyer J, Eikhom TS

Abstract

An endonuclease activity associated with purified proteinase K-treated intracisternal A-particles was identified and characterized. The activity required divalent cations, preferring Mn2+ to Mg2+. Salt concentrations above 50 mM inhibited the activity. The endonuclease was greatly stimulated by ATP, ADP, and dATP, whereas AMP appeared to produce a slight inhibition. GTP had no apparent effect on the activity. The enzyme introduced single-stranded nicks into DNA and nicked preferentially supercoiled DNA duplexes in the presence of ATP, although linear duplexes also functioned as substrates. Single-stranded DNA was not nicked to any great extent. The molecular weight of the enzyme was estimated to be about 40,000. The characteristics of this enzyme are very similar to those of the endonuclease found associated with Friend murine leukemia virus.

MeSH Terms
Adenosine Triphosphate/pharmacology Cations, Divalent/pharmacology DNA, Single-Stranded/metabolism DNA, Superhelical/metabolism Endonucleases/metabolism Endoplasmic Reticulum/microbiology Molecular Weight Retroviridae/enzymology,isolation & purification
Chemicals
Cations, Divalent DNA, Single-Stranded DNA, Superhelical Adenosine Triphosphate Endonucleases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Nissen-Meyer J
Eikhom T S
References (20)
20 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.40.3.927-931.1981
Published
1981-12-00
Pages
927-31
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC256704
Subset
IM
External Links
PubMed source DOI: 10.1128/JVI.40.3.927-931.1981 PMC Full Text View journal details
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