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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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Stephanou AS,Roberts GA,Tock MR,Pritchard EH,Turkington R,Nutley M,Cooper A,Dryden DT

doi

10.1016/j.bbrc.2008.11.014

subject

Has Abstract

pub_date

2009-01-02 00:00:00

pages

129-32

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(08)02196-7

journal_volume

378

pub_type

杂志文章

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