JBC Focus on PI3-Kinase with Echelon

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on January 19, 2001
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
276/4/2509    most recent
M007778200v1
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 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 Waidner, L. A.
Right arrow Articles by Karpel, R. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Waidner, L. A.
Right arrow Articles by Karpel, R. L.
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?

Papers In Press, published online ahead of print October 25, 2000
J. Biol. Chem, 10.1074/jbc.M007778200
Submitted on August 25, 2000
Revised on October 23, 2000
Accepted on October 24, 2000

Domain effects on the DNA-interactive properties of bacteriophage T4 gene 32 protein

Lisa A. Waidner, Elizabeth K. Flynn, Min Wu, Xing Li, and Richard L. Karpel

Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, MD 21250

Corresponding Author: karpel{at}umbc.edu

Bacteriophage T4 gene 32 protein, a model for single-strand specific nucleic acid binding proteins, consists of three structurally and functionally distinct domains. We have studied the effects of the N- and C- domains on the protein's structure and its nucleic acid-interactive properties. Although the presence of the C-domain decreases the proteolytic susceptibility of the core (central) domain, quenching of the core's tryptophan fluorescence by iodide is unaltered by the presence of the terminal domains. These results suggest that the overall conformation of the core domain remains largely independent of the flanking domains. Removal of the N- or the C-terminus does not abolish the protein's DNA renaturation activity. However, intact protein and its three truncated forms differ in DNA helix-destabilizing activity. The C-domain alone is responsible for the kinetic barrier to natural DNA helix destabilization seen with intact protein. Intact protein and core domain potentiate the DNA helix-destabilizing activity of truncated protein lacking only the C-domain ("*I"), enhancing the observed hyperchromicity while increasing the melting temperature. Proteolysis experiments suggest that the affinity of core domain for single-stranded DNA is increased in the presence of *I. We propose that *I can "mingle" with intact protein or core domain while bound to ssDNA.


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
S. W. Nelson, R. Kumar, and S. J. Benkovic
RNA Primer Handoff in Bacteriophage T4 DNA Replication: THE ROLE OF SINGLE-STRANDED DNA-BINDING PROTEIN AND POLYMERASE ACCESSORY PROTEINS
J. Biol. Chem., August 15, 2008; 283(33): 22838 - 22846.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. E. Jones, T. C. Mueser, and N. G. Nossal
Bacteriophage T4 32 Protein Is Required for Helicase-dependent Leading Strand Synthesis When the Helicase Is Loaded by the T4 59 Helicase-loading Protein
J. Biol. Chem., March 26, 2004; 279(13): 12067 - 12075.
[Abstract] [Full Text] [PDF]

Home page
 Microbiol. Mol. Biol. Rev.Home page
E. S. Miller, E. Kutter, G. Mosig, F. Arisaka, T. Kunisawa, and W. Ruger
Bacteriophage T4 Genome
Microbiol. Mol. Biol. Rev., March 1, 2003; 67(1): 86 - 156.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.