JBC

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


     

This Article
Right arrow Full Text (PDF)
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 Weiner, J. H.
Right arrow Articles by Kornberg, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Weiner, J. H.
Right arrow Articles by Kornberg, A.
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?

JBC, Vol. 250, Issue 6, 1972-1980, Mar, 1975

The deoxyribonucleic acid unwinding protein of Escherichia coli. Properties and functions in replication

J. H. Weiner, L. L. Bertsch and A. Kornberg

The DNA unwinding protein of Escherichia coli (Sigal, N., Delius, H., Kornberg, T., Gefter, M., and Alberts, B. (1972) Proc. Nat. Acad. Sci. U.S.A. 69, 3537-3541) has been purified to homogeneity by a simple procedure which utilizes its stability to heating. The protein is an asymmetric tetramer of 18,500 dalton subunits which binds preferentially to single-stranded DNA at a ratio of one protein molecule per 32 nucleotides. Binding to DNA is complete in less than 10 s at 0 degrees while release of the protein from single-stranded DNA is relatively slow even at 37 degrees. A simple functional assay for unwinding protein depends on its essential role in the conversion of phage G4 single-stranded DNA to the replicative form. Unwinding protein stimulates initiation of replication of all single-stranded phage DNAs. Approximately 300 copies of unwinding protein are present per cell, as estimated by antibody titration, an amount sufficient to cover substantial lengths of DNA in several replicating forks.
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
R. D. Shereda, D. A. Bernstein, and J. L. Keck
A Central Role for SSB in Escherichia coli RecQ DNA Helicase Function
J. Biol. Chem., June 29, 2007; 282(26): 19247 - 19258.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Z.-G. He, L. F. Rezende, S. Willcox, J. D. Griffith, and C. C. Richardson
The Carboxyl-terminal Domain of Bacteriophage T7 Single-stranded DNA-binding Protein Modulates DNA Binding and Interaction with T7 DNA Polymerase
J. Biol. Chem., August 8, 2003; 278(32): 29538 - 29545.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Sengupta, B.-C. Jang, M.-T. Wu, J.-H. Paik, H. Furneaux, and T. Hla
The RNA-binding Protein HuR Regulates the Expression of Cyclooxygenase-2
J. Biol. Chem., June 27, 2003; 278(27): 25227 - 25233.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. F. Rezende, T. Hollis, T. Ellenberger, and C. C. Richardson
Essential Amino Acid Residues in the Single-stranded DNA-binding Protein of Bacteriophage T7. IDENTIFICATION OF THE DIMER INTERFACE
J. Biol. Chem., December 20, 2002; 277(52): 50643 - 50653.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. S. Reddy, N. Guhan, and K. Muniyappa
Characterization of Single-stranded DNA-binding Proteins from Mycobacteria. THE CARBOXYL-TERMINAL DOMAIN OF SSB IS ESSENTIAL FOR STABLE ASSOCIATION WITH ITS COGNATE RecA PROTEIN
J. Biol. Chem., November 30, 2001; 276(49): 45959 - 45968.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
P. Handa, N. Acharya, S. Thanedar, K. Purnapatre, and U. Varshney
Distinct properties of Mycobacterium tuberculosis single-stranded DNA binding protein and its functional characterization in Escherichia coli
Nucleic Acids Res., October 1, 2000; 28(19): 3823 - 3829.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. Kong and C. C. Richardson
Role of the Acidic Carboxyl-terminal Domain of the Single-stranded DNA-binding Protein of Bacteriophage T7 in Specific Protein-Protein Interactions
J. Biol. Chem., March 13, 1998; 273(11): 6556 - 6564.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
P. Ward, F. B. Dean, M. E. O'Donnell, and K. I. Berns
Role of the Adenovirus DNA-Binding Protein in In Vitro Adeno-Associated Virus DNA Replication
J. Virol., January 1, 1998; 72(1): 420 - 427.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. Skaliter, M. Bergstein, and Z. Livneh
beta*, a UV-inducible Shorter Form of the beta Subunit of DNA Polymerase III of Escherichia coli
J. Biol. Chem., February 2, 1996; 271(5): 2491 - 2496.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. N. Rigler and L. J. Romano
Differences in the Mechanism of Stimulation of T7 DNA Polymerase by Two Binding Modes of Escherichia coli Single-stranded DNA-binding Protein
J. Biol. Chem., April 14, 1995; 270(15): 8910 - 8919.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
P. Handa, N. Acharya, and U. Varshney
Chimeras between Single-stranded DNA-binding Proteins from Escherichia coli and Mycobacterium tuberculosis Reveal That Their C-terminal Domains Interact with Uracil DNA Glycosylases
J. Biol. Chem., May 11, 2001; 276(20): 16992 - 16997.
[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 © 1975 by the American Society for Biochemistry and Molecular Biology.