The nuclease specificity of the bacteriophage phi X174 A* protein

S. A. Langeveld; A. D. van Mansfeld; A. van der Ende; J. H. van de Pol; G. A. van Arkel; P. J. Weisbeek

doi:https://doi.org/10.1093/nar/9.3.545

The nuclease specificity of the bacteriophage phi X174 A* protein

S. A. Langeveld, A. D. van Mansfeld, A. van der Ende, J. H. van de Pol, G. A. van Arkel, P. J. Weisbeek

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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)

Original language	English
Pages (from-to)	545-562
Journal	Nucleic Acids Research
Volume	9
Issue number	3
DOIs	https://doi.org/10.1093/nar/9.3.545
Publication status	Published - 1981

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https://doi.org/10.1093/nar/9.3.545

Cite this

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title = "The nuclease specificity of the bacteriophage phi X174 A* protein",

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)",

author = "Langeveld, {S. A.} and {van Mansfeld}, {A. D.} and {van der Ende}, A. and {van de Pol}, {J. H.} and {van Arkel}, {G. A.} and Weisbeek, {P. J.}",

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T1 - The nuclease specificity of the bacteriophage phi X174 A* protein

AU - Langeveld, S. A.

AU - van Mansfeld, A. D.

AU - van der Ende, A.

AU - van de Pol, J. H.

AU - van Arkel, G. A.

AU - Weisbeek, P. J.

PY - 1981

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N2 - 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)

AB - 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)

U2 - https://doi.org/10.1093/nar/9.3.545

DO - https://doi.org/10.1093/nar/9.3.545

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