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

Stephanou, A.S., Roberts, G.A., Tock, M.R., Pritchard, E.H., Turkington, R., Nutley, M., Cooper, A. and Dryden, D.T.F. (2009) A mutational analysis of DNA mimicry by ocr, the gene 0.3 antirestriction protein of bacteriophage T7. Biochemical and Biophysical Research Communications, 378(1), pp. 129-132. (doi:10.1016/j.bbrc.2008.11.014)

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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.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Nutley, Mrs Margaret and Cooper, Professor Alan
Authors: Stephanou, A.S., Roberts, G.A., Tock, M.R., Pritchard, E.H., Turkington, R., Nutley, M., Cooper, A., and Dryden, D.T.F.
Subjects:Q Science > QD Chemistry
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Biochemical and Biophysical Research Communications
ISSN:0006-291X
ISSN (Online):1090-2104
Published Online:14 November 2008

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