JBC Anatrace, Inc.

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


     


Originally published In Press as doi:10.1074/jbc.M513844200 on March 3, 2006

J. Biol. Chem., Vol. 281, Issue 18, 12561-12567, May 5, 2006
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
281/18/12561    most recent
M513844200v1
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 Wieczorek, A.
Right arrow Articles by McHenry, C. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wieczorek, A.
Right arrow Articles by McHenry, C. S.

The NH2-terminal php Domain of the {alpha} Subunit of the Escherichia coli Replicase Binds the {epsilon} Proofreading Subunit*

Anna Wieczorek and Charles S. McHenry1

From the Department of Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center, Denver, Colorado 80262

The {alpha} subunit of the replicase of all bacteria contains a php domain, initially identified by its similarity to histidinol phosphatase but of otherwise unknown function (Aravind, L., and Koonin, E. V. (1998) Nucleic Acids Res. 26, 3746-3752). Deletion of 60 residues from the NH2 terminus of the {alpha} php domain destroys {epsilon} binding. The minimal 255-residue php domain, estimated by sequence alignment with homolog YcdX, is insufficient for {epsilon} binding. However, a 320-residue segment including sequences that immediately precede the polymerase domain binds {epsilon} with the same affinity as the 1160-residue full-length {alpha} subunit. A subset of mutations of a conserved acidic residue (Asp43 in Escherichia coli {alpha}) present in the php domain of all bacterial replicases resulted in defects in {epsilon} binding. Using sequence alignments, we show that the prototypical Gram(+) Pol C, which contains the polymerase and proofreading activities within the same polypeptide chain, has an {epsilon}-like sequence inserted in a surface loop near the center of the homologous YcdX protein. These findings suggest that the php domain serves as a platform to enable coordination of proofreading and polymerase activities during chromosomal replication.


Received for publication, December 28, 2005 , and in revised form, February 27, 2006.

* This work was supported by Research Grant GM060273 from the National Institutes of Health. 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 To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center, 4200 East Ninth Ave., B-121, Denver, CO 80262. E-mail: Charles.McHenry{at}uchsc.edu.




This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
T. W. Kirby, S. Harvey, E. F. DeRose, S. Chalov, A. K. Chikova, F. W. Perrino, R. M. Schaaper, R. E. London, and L. C. Pedersen
Structure of the Escherichia coli DNA Polymerase III {epsilon}-HOT Proofreading Complex
J. Biol. Chem., December 15, 2006; 281(50): 38466 - 38471.
[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 © 2006 by the American Society for Biochemistry and Molecular Biology.