HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 279, Issue 7, 6027-6034, February 13, 2004

This Article Full Text Full Text (PDF) All Versions of this Article: 279/7/6027    most recent M310917200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Sharma, S. Articles by Wickner, S. Search for Related Content PubMed PubMed Citation Articles by Sharma, S. Articles by Wickner, S. Social Bookmarking                      What's this?

Plasmid P1 RepA Is Homologous to the F Plasmid RepE Class of Initiators^*

Suveena Sharma, Bangalore K. Sathyanarayana, Jeremy G. Bird, Joel R. Hoskins, Byungkook Lee, and Sue Wickner

From the Laboratory of Molecular Biology, NCI, National Institutes of Health, Bethesda, Maryland 20892

DNA replication of plasmid P1 requires a plasmid-encoded origin DNA-binding protein, RepA. RepA is an inactive dimer and is converted by molecular chaperones into an active monomer that binds RepA binding sites. Although the sequence of RepA is not homologous to that of F plasmid RepE, we found by using fold-recognition programs that RepA shares structural homology with RepE and built a model based on the RepE crystal structure. We constructed mutants in the two predicted DNA binding domains to test the model. As expected, the mutants were defective in P1 DNA binding. The model predicted that RepA binds the first half of the binding site through interactions with the C-terminal DNA binding domain and the second half through interactions with the N-terminal domain. The experiments supported the prediction. The model was further supported by the observation that mutants defective in dimerization map to the predicted subunit interface region, based on the crystal structure of pPS10 RepA, a RepE family member. These results suggest P1 RepA is structurally homologous to plasmid initiators, including those of F, R6K, pSC101, pCU1, pPS10, pFA3, pGSH500, Rts1, RepHI1B, RepFIB, and RSF1010.

Received for publication, October 3, 2003 , and in revised form, November 20, 2003.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

These authors contributed equally to this work.

To whom correspondence should be addressed: Bldg. 37, Rm. 5144, NCI, National Institutes of Health, 37 Convent Dr. MSC37-4264, Bethesda, MD 20892-4264. Tel.: 301-496-2629; Fax: 301-402-1344; E-mail: suewick{at}helix.nih.gov

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				A. Nakamura, C. Wada, and K. Miki Structural basis for regulation of bifunctional roles in replication initiator protein PNAS, November 20, 2007; 104(47): 18484 - 18489. [Abstract] [Full Text] [PDF]

				M. Tang, D. K. Bideshi, H.-W. Park, and B. A. Federici Iteron-Binding ORF157 and FtsZ-Like ORF156 Proteins Encoded by pBtoxis Play a Role in Its Replication in Bacillus thuringiensis subsp. israelensis J. Bacteriol., November 15, 2007; 189(22): 8053 - 8058. [Abstract] [Full Text] [PDF]

				S. Kunnimalaiyaan, S. A. Rakowski, and M. Filutowicz Structure-Based Functional Analysis of the Replication Protein of Plasmid R6K: Key Amino Acids at the {pi}/DNA Interface J. Bacteriol., July 1, 2007; 189(13): 4953 - 4956. [Abstract] [Full Text] [PDF]

				M. Han, M. Yagura, and T. Itoh Specific Interaction between the Initiator Protein (Rep) and Origin of Plasmid ColE2-P9 J. Bacteriol., February 1, 2007; 189(3): 1061 - 1071. [Abstract] [Full Text] [PDF]

				M. K. Swan, D. Bastia, and C. Davies Crystal structure of {pi} initiator protein-iteron complex of plasmid R6K: Implications for initiation of plasmid DNA replication PNAS, December 5, 2006; 103(49): 18481 - 18486. [Abstract] [Full Text] [PDF]

				S. Kunnimalaiyaan, R. B. Inman, S. A. Rakowski, and M. Filutowicz Role of {pi} Dimers in Coupling ("Handcuffing") of Plasmid R6K's {gamma} ori Iterons J. Bacteriol., June 1, 2005; 187(11): 3779 - 3785. [Abstract] [Full Text] [PDF]

				N. Das, M. Valjavec-Gratian, A. N. Basuray, R. A. Fekete, P. P. Papp, J. Paulsson, and D. K. Chattoraj Multiple homeostatic mechanisms in the control of P1 plasmid replication PNAS, February 22, 2005; 102(8): 2856 - 2861. [Abstract] [Full Text] [PDF]

				R. A. Slavcev and B. E. Funnell Identification and Characterization of a Novel Allele of Escherichia coli dnaB Helicase That Compromises the Stability of Plasmid P1 J. Bacteriol., February 15, 2005; 187(4): 1227 - 1237. [Abstract] [Full Text] [PDF]

				S. Kunnimalaiyaan, R. Kruger, W. Ross, S. A. Rakowski, and M. Filutowicz Binding Modes of the Initiator and Inhibitor Forms of the Replication Protein {pi} to the {gamma} ori Iteron of Plasmid R6K J. Biol. Chem., September 24, 2004; 279(39): 41058 - 41066. [Abstract] [Full Text] [PDF]

				T. Betteridge, J. Yang, A. J. Pittard, and J. Praszkier Role of RepA and DnaA Proteins in the Opening of the Origin of DNA Replication of an IncB Plasmid J. Bacteriol., June 15, 2004; 186(12): 3785 - 3793. [Abstract] [Full Text] [PDF]