Nucleic Acids Res. 1979 Dec 20;7(8):2177-88.

Cleavage of single-stranded DNA by the A and A* proteins of bacteriophage phi X174.

Langeveld SA, van Mansfeld AD, de Winter JM, Weisbeek PJ.

Abstract

The purified A protein and A* protein of bacteriophage phi X174 have been tested for endonuclease activity on single stranded viral phi X174 DNA. The A protein (55.000 daltons) nicks single-stranded DNA in the same way and at the same place as it does superhelical RFI DNA, at the origin of DNA replication. The A* protein (37.000 daltons) can cleave the single-stranded viral DNA at many different sites. It has however a strong preference for the origin of replication. Both proteins generate 3'OH ends and blocked 5' termini at the nick site.

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The nuclease specificity of the bacteriophage phi X174 A* protein. [Nucleic Acids Res. 1981]
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Langeveld SA, van Mansfeld AD, van der Ende A, van de Pol JH, van Arkel GA, Weisbeek PJ. Nucleic Acids Res. 1981 Feb 11; 9(3):545-62.
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Cited by 17 PubMed Central articles

Cleavage of single-stranded DNA by the varphiX174 A protein: The A-single-stranded DNA covalent linkage. [Proc Natl Acad Sci U S A. 1984]
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Sanhueza S, Eisenberg S. Proc Natl Acad Sci U S A. 1984 Jul; 81(14):4285-9.
The A* protein of phi X174 is an inhibitor of DNA replication. [Nucleic Acids Res. 1981]
The A* protein of phi X174 is an inhibitor of DNA replication.
Eisenberg S, Ascarelli R. Nucleic Acids Res. 1981 Apr 24; 9(8):1991-2002.
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Cleavage of single-stranded DNA by the A and A* proteins of bacteriophage phi X174.

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