JBC Advanced Glycation Endproducts

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M109312200 on December 10, 2001

J. Biol. Chem., Vol. 277, Issue 8, 6733-6742, February 22, 2002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
277/8/6733    most recent
M109312200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Serna-Rico, A.
Right arrow Articles by Meijer, W. J. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Serna-Rico, A.
Right arrow Articles by Meijer, W. J. J.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

The Bacillus subtilis Phage phi 29 Protein p16.7, Involved in phi 29 DNA Replication, Is a Membrane-localized Single-stranded DNA-binding Protein*

Alejandro Serna-RicoDagger , Margarita Salas§, and Wilfried J. J. Meijer

From the Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain

The functional role of the phi 29-encoded integral membrane protein p16.7 in phage DNA replication was studied using a soluble variant, p16.7A, lacking the N-terminal membrane-spanning domain. Because of the protein-primed mechanism of DNA replication, the bacteriophage phi 29 replication intermediates contain long stretches of single-stranded DNA (ssDNA). Protein p16.7A was found to be an ssDNA-binding protein. In addition, by direct and functional analysis we show that protein p16.7A binds to the stretches of ssDNA of the phi 29 DNA replication intermediates. Properties of protein p16.7A were compared with those of the phi 29-encoded single-stranded DNA-binding protein p5. The results obtained show that both proteins have different, non-overlapping functions. The likely role of p16.7 in attaching phi 29 DNA replication intermediates to the membrane of the infected cell is discussed. Homologues of gene 16.7 are present in phi 29-related phages, suggesting that the proposed role of p16.7 is conserved in this family of phages.


* This investigation was supported by National Institutes of Health Research Grant 2R01 GM27242-22, Dirección General de Investigación Científica y Técnica Grant PB98-0645, European Economic Community Grant ERBFMX CT97 0125, and an Institutional grant from Fundación Ramón Areces.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Holder of a predoctoral fellowship from Gobierno Vasco.

§ To whom correspondence should be addressed: Tel.: 34 91 397 8435; Fax: 34 91 397 8490; E-mail: Msalas@cbm.uam.es.

Supported by a postdoctoral fellowship from the Spanish Ministry of Education and Culture.


Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Bacteriol.Home page
M. Alcorlo, V. Gonzalez-Huici, J. M. Hermoso, W. J. J. Meijer, and M. Salas
The Phage {phi}29 Membrane Protein p16.7, Involved in DNA Replication, Is Required for Efficient Ejection of the Viral Genome
J. Bacteriol., August 1, 2007; 189(15): 5542 - 5549.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. Munoz-Espin, M. A. Fuertes, M. Jimenez, L. Villar, C. Alonso, G. Rivas, M. Salas, and W. J. J. Meijer
Structural and Functional Analysis of {varphi}29 p16.7C Dimerization Mutants: IDENTIFICATION OF A NOVEL AROMATIC CAGE DIMERIZATION MOTIF
J. Biol. Chem., June 1, 2007; 282(22): 16521 - 16531.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. L. Asensio, A. Albert, D. Munoz-Espin, C. Gonzalez, J. Hermoso, L. Villar, J. Jimenez-Barbero, M. Salas, and W. J. J. Meijer
Structure of the Functional Domain of {varphi}29 Replication Organizer: INSIGHTS INTO OLIGOMERIZATION AND DNA BINDING
J. Biol. Chem., May 27, 2005; 280(21): 20730 - 20739.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. Munoz-Espin, M. G. Mateu, L. Villar, A. Marina, M. Salas, and W. J. J. Meijer
Phage {varphi}29 DNA Replication Organizer Membrane Protein p16.7 Contains a Coiled Coil and a Dimeric, Homeodomain-related, Functional Domain
J. Biol. Chem., November 26, 2004; 279(48): 50437 - 50445.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
W. J. J. Meijer and M. Salas
Relevance of UP elements for three strong Bacillus subtilis phage {phi}29 promoters
Nucleic Acids Res., February 18, 2004; 32(3): 1166 - 1176.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.