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

J. Biol. Chem., Vol. 277, Issue 17, 14575-14580, April 26, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/17/14575    most recent M110759200v1 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 Becker, E. C. Articles by Meyer, R. J. Search for Related Content PubMed PubMed Citation Articles by Becker, E. C. Articles by Meyer, R. J. Social Bookmarking                      What's this?

MobA, the DNA Strand Transferase of Plasmid R1162
THE MINIMAL DOMAIN REQUIRED FOR DNA PROCESSING AT THE ORIGIN OF TRANSFER^*

Eric C. Becker and Richard J. Meyer^§

From the Section of Molecular Genetics and Microbiology, School of Biology and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712

MobA is a DNA strand transferase encoded by the plasmid R1162 and required for plasmid DNA processing during conjugal transfer. The smallest active fragment was identified using phage display and partial enzymatic digestion of the purified protein. This fragment, consisting of approximately the first 184 amino acids, is able to bind and cleave its normal DNA substrate, the origin of transfer (oriT). Smaller fragments having one of these activities were not obtained. An active intermediate consisting of MobA linked to DNA was isolated and used to show that a single molecule of MobA is sufficient to carry out all of the DNA processing steps during transfer. These results, along with those obtained earlier, point to a single large, active site in MobA that makes several different contacts along the oriT DNA strand.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				R. Vignoli, N. F. Cordeiro, V. Garcia, M. I. Mota, L. Betancor, P. Power, J. A. Chabalgoity, F. Schelotto, G. Gutkind, and J. A. Ayala New TEM-Derived Extended-Spectrum {beta}-Lactamase and Its Genomic Context in Plasmids from Salmonella enterica Serovar Derby Isolates from Uruguay Antimicrob. Agents Chemother., February 1, 2006; 50(2): 781 - 784. [Abstract] [Full Text] [PDF]

				S. Jandle and R. Meyer Stringent and Relaxed Recognition of oriT by Related Systems for Plasmid Mobilization: Implications for Horizontal Gene Transfer J. Bacteriol., January 15, 2006; 188(2): 499 - 506. [Abstract] [Full Text] [PDF]

				M. C. A. Smith and C. D. Thomas An Accessory Protein Is Required for Relaxosome Formation by Small Staphylococcal Plasmids J. Bacteriol., June 1, 2004; 186(11): 3363 - 3373. [Abstract] [Full Text] [PDF]

				N. Furuya and T. Komano NikAB- or NikB-Dependent Intracellular Recombination between Tandemly Repeated oriT Sequences of Plasmid R64 in Plasmid or Single-Stranded Phage Vectors J. Bacteriol., July 1, 2003; 185(13): 3871 - 3877. [Abstract] [Full Text] [PDF]

				E. C. Becker and R. J. Meyer Relaxed Specificity of the R1162 Nickase: a Model for Evolution of a System for Conjugative Mobilization of Plasmids J. Bacteriol., June 15, 2003; 185(12): 3538 - 3546. [Abstract] [Full Text] [PDF]

				E. Grohmann, G. Muth, and M. Espinosa Conjugative Plasmid Transfer in Gram-Positive Bacteria Microbiol. Mol. Biol. Rev., June 1, 2003; 67(2): 277 - 301. [Abstract] [Full Text] [PDF]