Skip Navigation

This Article
Right arrow Print PDF (10951K)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
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 Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (12)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Zang, W.
Right arrow Articles by Evans, D. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zang, W.
Right arrow Articles by Evans, D. H.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1995, Vol. 23, No. 22 4620-4627
© 1995

Articles

DNA strand transfer catalyzed by the 5'-3' exonuclease domain of Escherichia coli DNA polymerase I

Wandong Zang+ and David H. Evans*

Department of Molecular Biology abd Genetics, The University of Guelph Guelph, Ontaruio, NIG 2W1, Canada

*To whom correspondence should be addressed

Received August 17, 1995. Accepted October 20, 1995.

A protein which promotes DNA strand transfer between linear double-stranded M13mp19 DNA and single-stranded viral M13mp19 DNA has been isolated from recA- E.coll. The protein is DNA polymerase I. Strand transfer activity resides in the small fragment encoding the 5'–3' exonuclease and can be detected using a recomblnant protein comprising the first 324 amino acids encoded by polA. Either the recombinant 5'–3' exonuclease or intact DNA polymerase I can catalyze joint molecule formation, in reactions requiring only Mg2+ and homologous DNA substrates. Both kinds of reactions are unaffected by added ATP. Electron microscopy shows that the joint molecules formed in these reactions bear displaced single strands and therefore this reaction is not simply promoted by annealing of exonuclease-gapped molecules. The pairing reaction is also polar and displaces the 5'-end of the non-complementary strand, extending the heteroduplex joint in a 5'-3' direction relative to the displaced strand. Thus strand transfer occurs with the same polarity as nick translation. These results show that E.coll, like many eukaryotes, possesses a protein which can promote ATP-independent strand-transfer reactions and raises questions concerning the possible biological role of this function.

+Present address: B.C.Cancer Reesearch Center, The University of British Columbia, 601 West10th Avenue, Vancouver, British Columbia, V5Z 1L3, Canada


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Bacteriol.Home page
H. B. Thomaides, E. J. Davison, L. Burston, H. Johnson, D. R. Brown, A. C. Hunt, J. Errington, and L. Czaplewski
Essential Bacterial Functions Encoded by Gene Pairs
J. Bacteriol., January 15, 2007; 189(2): 591 - 602.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Tseng, N. Palaniyar, W. Zhang, and D. H. Evans
DNA Binding and Aggregation Properties of the Vaccinia Virus I3L Gene Product
J. Biol. Chem., July 30, 1999; 274(31): 21637 - 21644.
[Abstract] [Full Text] [PDF]

Home page
 Microbiol. Mol. Biol. Rev.Home page
M. K. B. Berlyn
Linkage Map of Escherichia coli K-12, Edition 10: The Traditional Map
Microbiol. Mol. Biol. Rev., September 1, 1998; 62(3): 814 - 984.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.