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PMID: 6261225 Published · ppublish English Journal Article

The nuclease specificity of the bacteriophage phi X174 A* protein.

Nucleic acids research ·Vol. 9 ·No. 3 ·1981-02-11 ·Pages 545-62

Langeveld SA, van Mansfeld AD, van der Ende A, van de Pol JH, van Arkel GA, Weisbeek PJ

Abstract

The A* protein of bacteriophage phi X174 is a single-stranded DNA specific nuclease. It can cleave phi X viral ss DNA in many different places. The position of these sites have been determined within the known phi X174 nucleotide sequence (1). From the sequences at these sites it is clear that the A* protein recognizes and cleaves at sites that show only partial homology with the origin of RF DNA replication in the phi X DNA. Different parts of the origin sequence can be deduced that function as a signal for recognition and cleavage by the A* protein. We conclude that different parts within the DNA recognition domain of the A* protein are functional in the recognition of the origin sequence in single-stranded DNA. The existence of different DNA recognition domains in the A* protein, and therefore also in the A protein, leads to a model that can explain how the A protein performs its multiple function in the phi X174 DNA replication process (2).

MeSH Terms
Bacteriophage phi X 174/enzymology Base Sequence DNA Replication DNA Restriction Enzymes DNA, Single-Stranded/metabolism Deoxyribonucleases/metabolism Electrophoresis, Agar Gel Substrate Specificity Viral Proteins/metabolism Virus Replication
Chemicals
DNA, Single-Stranded Viral Proteins Deoxyribonucleases DNA Restriction Enzymes
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Langeveld S A
van Mansfeld A D
van der Ende A
van de Pol J H
van Arkel G A
Weisbeek P J
References (24)
24 references, click to expand
  1. Mutants of bacteriophage S13 blocked in infectious DNA synthesis.
    J Mol Biol. 1966 May;17(1):218-36 PMID: 5335755
  2. Formation of the parental replicative form DNA of bacteriophage phi-X174 and initial events in its replication.
    J Mol Biol. 1971 Nov 14;61(3):565-86 PMID: 5133115
  3. Two proteins of gene A of psiX174.
    Nat New Biol. 1973 Sep 5;245(140):6-8 PMID: 4516942
  4. Isolation and function of the gene A initiator of bacteriophage phi-chi 174, a highly specific DNA endonuclease.
    Proc Natl Acad Sci U S A. 1974 Apr;71(4):1549-53 PMID: 4598307
  5. Locating interrupted hydrogen bonding in the secondary structure of PM2 circular DNA by comparative denaturation mapping.
    J Virol. 1974 Jun;13(6):1176-85 PMID: 4833606
  6. Identification of a phiX174 coded protein involved in the shut-off of host DNA replication.
    Biochem Biophys Res Commun. 1975 Jul 8;65(1):323-30 PMID: 1096890
  7. Chain length determination of small double- and single-stranded DNA molecules by polyacrylamide gel electrophoresis.
    Biochemistry. 1975 Aug 26;14(17):3787-94 PMID: 1174504
  8. 'Single-stranded' DNA from phiX174 and M13 is cleaved by certain restriction endonucleases.
    Nature. 1975 Oct 2;257(5525):421-2 PMID: 809717
  9. Isolation and characterization of the protein coded by gene A of bacteriophage phiX174 DNA.
    Proc Natl Acad Sci U S A. 1976 Aug;73(8):2669-73 PMID: 1066678
  10. A new method for sequencing DNA.
    Proc Natl Acad Sci U S A. 1977 Feb;74(2):560-4 PMID: 265521
  11. Nucleotide sequence of bacteriophage phi X174 DNA.
    Nature. 1977 Feb 24;265(5596):687-95 PMID: 870828
  12. DNA sequence at the C termini of the overlapping genes A and B in bacteriophage phi X174.
    Nature. 1977 Feb 24;265(5596):702-5 PMID: 859575
  13. Bacteriophage phiX174: gene A overlaps gene B.
    Proc Natl Acad Sci U S A. 1977 Jun;74(6):2504-8 PMID: 267943
  14. phiX174 cistron A protein is a multifunctional enzyme in DNA replication.
    Proc Natl Acad Sci U S A. 1977 Aug;74(8):3198-202 PMID: 269383
  15. Nucleotide sequence of the origin of replication in bacteriophage phiX174 RF DNA.
    Nature. 1978 Feb 2;271(5644):417-20 PMID: 628424
  16. Nucleotide sequences of the separate origins of synthesis of bacteriophage G4 viral and complementary DNA strands.
    Proc Natl Acad Sci U S A. 1978 Mar;75(3):1081-5 PMID: 274698
  17. Purification and characterization of phiX174 gene A protein. A multifunctional enzyme of duplex DNA replication.
    J Biol Chem. 1979 Jun 25;254(12):5328-32 PMID: 447653
  18. Role of polymeric forms of the bacteriophage phi X174 coded gene A protein in phi XRFI DNA cleavage.
    J Biol Chem. 1979 Oct 10;254(19):9416-28 PMID: 158588
  19. Cleavage of single-stranded DNA by the A and A* proteins of bacteriophage phi X174.
    Nucleic Acids Res. 1979 Dec 20;7(8):2177-88 PMID: 160544
  20. Improved method for the isolation of the A and A* proteins of bacteriophage phi X174.
    FEBS Lett. 1980 Jun 2;114(2):269-72 PMID: 6248369
  21. Intercistronic regions in phi X174 DNA. II. Biochemical and biological analysis of mutants with altered intercistronic regions between genes J and F.
    J Mol Biol. 1980 Jul 25;141(1):25-41 PMID: 6253647
  22. Studies of the recognition sequence of phi X174 gene A protein. Cleavage site of phi X gene A protein in St-1 RFI DNA.
    Nucleic Acids Res. 1980 May 10;8(9):2009-21 PMID: 6253953
  23. Origin of DNA replication of bacteriophage f1 as the signal for termination.
    Proc Natl Acad Sci U S A. 1980 Sep;77(9):5226-9 PMID: 6254068
  24. Cleavage of phi X174 single-stranded DNA by gene A protein and formation of a tight protein-DNA complex.
    J Virol. 1980 Aug;35(2):409-13 PMID: 6449606
Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/9.3.545
Published
1981-02-11
Pages
545-62
Language
English
Region
England
NLM ID
0411011
PMCID
PMC327221
Subset
IM
External Links
PubMed source DOI: 10.1093/nar/9.3.545 PMC Full Text View journal details
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