Open AccessThe nuclease specificity of the bacteriophage øX174 A*protein
Author(s) -
S.A. Langeveld,
A.D.M. van Mansfeld,
Arie van der Ende,
J.H. van de Pol,
G.A. van Arkel,
Peter Weisbeek
Publication year - 1981
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/9.3.545
Subject(s) - biology , dna , dna replication , nuclease , recognition sequence , microbiology and biotechnology , hmg box , bacteriophage , dna clamp , genetics , dna binding protein , gene , rna , restriction enzyme , escherichia coli , reverse transcriptase , transcription factor
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).
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