JBC Transcription and Nuclear Factor Monoclonals

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


     


Originally published In Press as doi:10.1074/jbc.M006556200 on August 17, 2000

J. Biol. Chem., Vol. 275, Issue 44, 34757-34765, November 3, 2000
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
275/44/34757    most recent
M006556200v1
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 Li, X.
Right arrow Articles by Marians, K. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Li, X.
Right arrow Articles by Marians, K. 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?

Two Distinct Triggers for Cycling of the Lagging Strand Polymerase at the Replication Fork*

Xiaojun Li and Kenneth J. Marians

From the Molecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021

There are two modes of DNA synthesis at a replication fork. The leading strand is synthesized in a continuous fashion in lengths that in Escherichia coli can be in excess of 2 megabases. On the other hand, the lagging strand is synthesized in relatively short stretches of 2 kilobases. Nevertheless, identical assemblies of the DNA polymerase III core tethered to the beta  sliding clamp account for both modes of DNA synthesis. Yet the same lagging strand polymerase accounts for the synthesis of all Okazaki fragments at a replication fork, cycling repeatedly every 1 or 2 s from the 3'-end of the just-completed fragment to the 3'-end of the new primer. Several models have been invoked to account for the rapid cycling of a polymerase complex that can remain bound to the template for upward of 40 min. By using isolated replication protein-DNA template complexes, we have tested these models and show here that cycling of the lagging strand polymerase can be triggered by either the action of primase binding to the replisome and synthesizing a primer or by collision of the lagging strand polymerase with the 5'-end of the previous Okazaki fragment.


* This work was supported by National Institutes of Health Grant GM34557.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.


Copyright © 2000 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. Biol. Chem.Home page
A. Furukohri, M. F. Goodman, and H. Maki
A Dynamic Polymerase Exchange with Escherichia coli DNA Polymerase IV Replacing DNA Polymerase III on the Sliding Clamp
J. Biol. Chem., April 25, 2008; 283(17): 11260 - 11269.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
P. McInerney and M. O'Donnell
Replisome Fate upon Encountering a Leading Strand Block and Clearance from DNA by Recombination Proteins
J. Biol. Chem., August 31, 2007; 282(35): 25903 - 25916.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
C. D. Bayliss, W. A. Sweetman, and E. R. Moxon
Destabilization of tetranucleotide repeats in Haemophilus influenzae mutants lacking RnaseHI or the Klenow domain of PolI
Nucleic Acids Res., January 14, 2005; 33(1): 400 - 408.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
P. McInerney and M. O'Donnell
Functional Uncoupling of Twin Polymerases: MECHANISM OF POLYMERASE DISSOCIATION FROM A LAGGING-STRAND BLOCK
J. Biol. Chem., May 14, 2004; 279(20): 21543 - 21551.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
S. A. Taft-Benz and R. M. Schaaper
The {theta} Subunit of Escherichia coli DNA Polymerase III: a Role in Stabilizing the {varepsilon} Proofreading Subunit
J. Bacteriol., May 1, 2004; 186(9): 2774 - 2780.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
N. Costantino and D. L. Court
Enhanced levels of {lambda} Red-mediated recombinants in mismatch repair mutants
PNAS, December 23, 2003; 100(26): 15748 - 15753.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. M. Bullard, A. E. Pritchard, M.-S. Song, B. P. Glover, A. Wieczorek, J. Chen, N. Janjic, and C. S. McHenry
A Three-domain Structure for the delta Subunit of the DNA Polymerase III Holoenzyme delta Domain III Binds delta ' and Assembles into the DnaX Complex
J. Biol. Chem., April 5, 2002; 277(15): 13246 - 13256.
[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 © 2000 by the American Society for Biochemistry and Molecular Biology.