A mutational analysis of DNA mimicry by ocr, the gene 0.3 antirestriction protein of bacteriophage T7

Augoustinos S. Stephanou; Gareth A. Roberts; Mark R. Tock; Emily H. Pritchard; Rachel Turkington; Margaret Nutley; Alan Cooper; David T. F. Dryden

doi:10.1016/j.bbrc.2008.11.014

A mutational analysis of DNA mimicry by ocr, the gene 0.3 antirestriction protein of bacteriophage T7

Augoustinos S. Stephanou, Gareth A. Roberts, Mark R. Tock, Emily H. Pritchard, Rachel Turkington, Margaret Nutley, Alan Cooper, David T. F. Dryden

Research output: Contribution to journal › Article › peer-review

Abstract / Description of output

The ocr protein of bacteriophage T7 is a structural and electrostatic mimic of approximately 24 base pairs of double-stranded B-form DNA. As such, it inhibits all Type I restriction and modification (R/M) enzymes by blocking their DNA binding grooves and inactivates them. This allows the infection of the bacterial cell by T7 to proceed unhindered by the action of the R/M defence system. We have mutated aspartate and glutamate residues on the surface of ocr to investigate their contribution to the tight binding between the EcoKI Type I R/M enzyme and ocr. Contrary to expectations, all of the single and double site mutations of ocr constructed were active as anti-R/M proteins in vivo and in vitro indicating that the mimicry of DNA by ocr is very resistant to change. (C) 2008 Elsevier Inc. All rights reserved.

Original language	English
Pages (from-to)	129-132
Number of pages	4
Journal	Biochemical and Biophysical Research Communications
Volume	378
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2008.11.014
Publication status	Published - 2 Jan 2009

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title = "A mutational analysis of DNA mimicry by ocr, the gene 0.3 antirestriction protein of bacteriophage T7",

abstract = "The ocr protein of bacteriophage T7 is a structural and electrostatic mimic of approximately 24 base pairs of double-stranded B-form DNA. As such, it inhibits all Type I restriction and modification (R/M) enzymes by blocking their DNA binding grooves and inactivates them. This allows the infection of the bacterial cell by T7 to proceed unhindered by the action of the R/M defence system. We have mutated aspartate and glutamate residues on the surface of ocr to investigate their contribution to the tight binding between the EcoKI Type I R/M enzyme and ocr. Contrary to expectations, all of the single and double site mutations of ocr constructed were active as anti-R/M proteins in vivo and in vitro indicating that the mimicry of DNA by ocr is very resistant to change. (C) 2008 Elsevier Inc. All rights reserved.",

author = "Stephanou, {Augoustinos S.} and Roberts, {Gareth A.} and Tock, {Mark R.} and Pritchard, {Emily H.} and Rachel Turkington and Margaret Nutley and Alan Cooper and Dryden, {David T. F.}",

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T1 - A mutational analysis of DNA mimicry by ocr, the gene 0.3 antirestriction protein of bacteriophage T7

AU - Stephanou, Augoustinos S.

AU - Roberts, Gareth A.

AU - Tock, Mark R.

AU - Pritchard, Emily H.

AU - Turkington, Rachel

AU - Nutley, Margaret

AU - Cooper, Alan

AU - Dryden, David T. F.

PY - 2009/1/2

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N2 - The ocr protein of bacteriophage T7 is a structural and electrostatic mimic of approximately 24 base pairs of double-stranded B-form DNA. As such, it inhibits all Type I restriction and modification (R/M) enzymes by blocking their DNA binding grooves and inactivates them. This allows the infection of the bacterial cell by T7 to proceed unhindered by the action of the R/M defence system. We have mutated aspartate and glutamate residues on the surface of ocr to investigate their contribution to the tight binding between the EcoKI Type I R/M enzyme and ocr. Contrary to expectations, all of the single and double site mutations of ocr constructed were active as anti-R/M proteins in vivo and in vitro indicating that the mimicry of DNA by ocr is very resistant to change. (C) 2008 Elsevier Inc. All rights reserved.

AB - The ocr protein of bacteriophage T7 is a structural and electrostatic mimic of approximately 24 base pairs of double-stranded B-form DNA. As such, it inhibits all Type I restriction and modification (R/M) enzymes by blocking their DNA binding grooves and inactivates them. This allows the infection of the bacterial cell by T7 to proceed unhindered by the action of the R/M defence system. We have mutated aspartate and glutamate residues on the surface of ocr to investigate their contribution to the tight binding between the EcoKI Type I R/M enzyme and ocr. Contrary to expectations, all of the single and double site mutations of ocr constructed were active as anti-R/M proteins in vivo and in vitro indicating that the mimicry of DNA by ocr is very resistant to change. (C) 2008 Elsevier Inc. All rights reserved.

U2 - 10.1016/j.bbrc.2008.11.014

DO - 10.1016/j.bbrc.2008.11.014

M3 - Article

SN - 0006-291X

VL - 378

SP - 129

EP - 132

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

A mutational analysis of DNA mimicry by ocr, the gene 0.3 antirestriction protein of bacteriophage T7

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