This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Odegrip, R.
Right arrow Articles by Chattoraj, D. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Odegrip, R.
Right arrow Articles by Chattoraj, D. K.

 Previous Article  |  Next Article 

Journal of Virology, May 2000, p. 4057-4063, Vol. 74, No. 9
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The Interaction of Bacteriophage P2 B Protein with Escherichia coli DnaB Helicase

Richard Odegrip,1 Stephan Schoen,1 Elisabeth Haggård-Ljungquist,1,* Kyusung Park,2 and Dhruba K. Chattoraj2

Department of Genetics, Stockholm University, S-10691 Stockholm, Sweden,1 and Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892-42552

Received 21 September 1999/Accepted 26 January 2000

Bacteriophage P2 requires several host proteins for lytic replication, including helicase DnaB but not the helicase loader, DnaC. Some genetic studies have suggested that the loading is done by a phage-encoded protein, P2 B. However, a P2 minichromosome containing only the P2 initiator gene A and a marker gene can be established as a plasmid without requiring the P2 B gene. Here we demonstrate that P2 B associates with DnaB. This was done by using the yeast two-hybrid system in vivo and was confirmed in vitro, where 35S-labeled P2 B bound specifically to DnaB adsorbed to Q Sepharose beads and monoclonal antibodies directed against the His-tagged P2 B protein were shown to coprecipitate the DnaB protein. Finally, P2 B was shown to stabilize the opening of a reporter origin, a reaction that is facilitated by the inactivation of DnaB. In this respect, P2 B was comparable to lambda  P protein, which is known to be capable of binding and inactivating the helicase while acting as a helicase loader. Even though P2 B has little similarity to other known or predicted helicase loaders, we suggest that P2 B is required for efficient loading of DnaB and that this role, although dispensable for P2 plasmid replication, becomes essential for P2 lytic replication.

* Corresponding author. Mailing address: Dept. of Genetics, Stockholm University, S-10691 Stockholm, Sweden. Phone: 46-8-161270. Fax: 46-8-164315. E-mail: Elisabeth.Haggard{at}genetics.su.se.

Journal of Virology, May 2000, p. 4057-4063, Vol. 74, No. 9
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Haaber, J., Rousseau, G. M., Hammer, K., Moineau, S. (2009). Identification and Characterization of the Phage Gene sav, Involved in Sensitivity to the Lactococcal Abortive Infection Mechanism AbiV. Appl. Environ. Microbiol. 75: 2484-2494 [Abstract] [Full Text]  
  • Biswas, E. E., Barnes, M. H., Moir, D. T., Biswas, S. B. (2009). An Essential DnaB Helicase of Bacillus anthracis: Identification, Characterization, and Mechanism of Action. J. Bacteriol. 191: 249-260 [Abstract] [Full Text]  
  • Zhong, Z., Helinski, D., Toukdarian, A. (2003). A Specific Region in the N Terminus of a Replication Initiation Protein of Plasmid RK2 Is Required for Recruitment of Pseudomonas aeruginosa DnaB Helicase to the Plasmid Origin. J. Biol. Chem. 278: 45305-45310 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»