Stable packaging of phage PRD1 DNA requires adsorption protein P2, which binds to the IncP plasmid-encoded conjugative transfer complex.

Abstract:

:The double-stranded DNA bacteriophage PRD1 uses an IncP plasmid-encoded conjugal transfer complex as a receptor. Plasmid functions in the PRD1 life cycle are restricted to phage adsorption and DNA entry. A single phage structural protein, P2, located at the fivefold capsid vertices, is responsible for PRD1 attachment to its host. The purified recombinant adsorption protein was judged to be monomeric by gel filtration, rate zonal centrifugation, analytical ultracentrifugation, and chemical cross-linking. It binds to its receptor with an apparent K(d) of 0.20 nM, and this binding prevents phage adsorption. P2-deficient particles are unstable and spontaneously release the DNA with concomitant formation of the tail-like structure originating from the phage membrane. We envisage the DNA to be packaged through one vertex, but the presence of P2 on the other vertices suggests a mechanism whereby the injection vertex is determined by P2 binding to the receptor.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Grahn AM,Caldentey J,Bamford JK,Bamford DH

doi

10.1128/JB.181.21.6689-6696.1999

keywords:

subject

Has Abstract

pub_date

1999-11-01 00:00:00

pages

6689-96

issue

21

eissn

0021-9193

issn

1098-5530

journal_volume

181

pub_type

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