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

J. Biol. Chem., Vol. 282, Issue 35, 25903-25916, August 31, 2007

This Article Full Text Full Text (PDF) All Versions of this Article: 282/35/25903    most recent M703777200v1 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 McInerney, P. Articles by O'Donnell, M. Search for Related Content PubMed PubMed Citation Articles by McInerney, P. Articles by O'Donnell, M. Social Bookmarking                      What's this?

Replisome Fate upon Encountering a Leading Strand Block and Clearance from DNA by Recombination Proteins^*

From the Howard Hughes Medical Institute, Laboratory of DNA Replication, Rockefeller University, New York, New York 10021

Replication forks that collapse upon encountering a leading strand lesion are reactivated by a recombinative repair process called replication restart. Using rolling circle DNA substrates to model replication forks, we examine the fate of the helicase and both DNA polymerases when the leading strand polymerase is blocked. We find that the helicase continues over 0.5 kb but less than 3 kb and that the lagging strand DNA polymerase remains active despite its connection to a stalled leading strand enzyme. Furthermore, the blocked leading strand polymerase remains stably bound to the replication fork, implying that it must be dismantled from DNA in order for replication restart to initiate. Genetic studies have identified at least four gene products required for replication restart, RecF, RecO, RecR, and RecA. We find here that these proteins displace a stalled polymerase at a DNA template lesion. Implications of these results for replication fork collapse and recovery are discussed.

Received for publication, May 8, 2007 , and in revised form, June 19, 2007.

^* This work was supported by National Institutes of Health Grants GM38839 and GM62540. 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.

¹ Present address: Helicos Biosciences Corp., Cambridge, MA 02139.

² To whom correspondence should be addressed: Howard Hughes Medical Institute, Laboratory of DNA Replication, 1230 York Ave., New York, NY 10021. Tel.: 212-327-7255; Fax: 212-327-7253; E-mail: odonnel{at}mail.rockefeller.edu.

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

This article has been cited by other articles:

				J. Atkinson and P. McGlynn Replication fork reversal and the maintenance of genome stability Nucleic Acids Res., June 1, 2009; 37(11): 3475 - 3492. [Abstract] [Full Text] [PDF]

				N. Willis and N. Rhind Mus81, Rhp51(Rad51), and Rqh1 Form an Epistatic Pathway Required for the S-Phase DNA Damage Checkpoint Mol. Biol. Cell, February 1, 2009; 20(3): 819 - 833. [Abstract] [Full Text] [PDF]