Functional identification of the DNA packaging terminase from Pseudomonas aeruginosa phage PaP3

Functional identification of the DNA packaging terminase from Pseudomonas aeruginosa phage PaP3 Terminase proteins are responsible for DNA recognition and initiation of DNA packaging in phages. We previously reported the genomic sequence of a temperate Pseudomonas aeruginosa phage, PaP3, and determined its precise integration site in the host bacterial chromosome. In this study, we present a detailed functional identification of the DNA packaging terminase for phage PaP3. The purified large subunit p03 was demonstrated to possess ATPase and nuclease activities, as well as the ability to bind to specific DNA when it is unassembled. In addition, a small terminase subunit (p01) of a new type was found and shown to bind specifically to cos -containing DNA and stimulate the cos -cleavage and ATPase activities of p03. The results presented here suggest that PaP3 utilizes a typical cos site mechanism for DNA packaging and provide a first step towards understanding the molecular mechanism of the PaP3 DNA packaging reaction. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

Functional identification of the DNA packaging terminase from Pseudomonas aeruginosa phage PaP3

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Publisher
Springer Journals
Copyright
Copyright © 2012 by Springer-Verlag Wien
Subject
Biomedicine; Medical Microbiology; Infectious Diseases; Virology
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s00705-012-1409-5
Publisher site
See Article on Publisher Site

Abstract

Terminase proteins are responsible for DNA recognition and initiation of DNA packaging in phages. We previously reported the genomic sequence of a temperate Pseudomonas aeruginosa phage, PaP3, and determined its precise integration site in the host bacterial chromosome. In this study, we present a detailed functional identification of the DNA packaging terminase for phage PaP3. The purified large subunit p03 was demonstrated to possess ATPase and nuclease activities, as well as the ability to bind to specific DNA when it is unassembled. In addition, a small terminase subunit (p01) of a new type was found and shown to bind specifically to cos -containing DNA and stimulate the cos -cleavage and ATPase activities of p03. The results presented here suggest that PaP3 utilizes a typical cos site mechanism for DNA packaging and provide a first step towards understanding the molecular mechanism of the PaP3 DNA packaging reaction.

Journal

Archives of VirologySpringer Journals

Published: Nov 1, 2012

References

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