| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 268, Issue 18, 13128-13136, 06, 1993
TR Hupp and JM Kaguni
A mutant form of DnaA protein encoded by the dnaA5 allele has been purified
and compared biochemically to its wild type counterpart. Biochemical
properties of DnaA5 protein include: 1) thermolabile activity in an oriC
plasmid replication system dependent on a crude enzyme fraction, 2)
comparable affinity relative to DnaA protein in binding to restriction
fragments containing either the Escherichia coli chromosomal origin, oriC,
or the dnaA promoter, 3) formation of a nucleoprotein complex similar to
DnaA protein at the DnaA boxes within the dnaA promoter as detected by
protection from DNase I cleavage, 4) formation of an altered nucleoprotein
complex with oriC as judged by DNase I protection experiments, 5)
inactivity in unwinding of oriC, 6) inactivity in oriC plasmid replication
systems dependent on purified enzymes, and 7) inhibition of DnaA protein by
addition of DnaA5 protein in assays of replication and of unwinding of
oriC, suggesting that mixed complexes formed between wild type and mutant
proteins are inactive.
DnaA5 protein is thermolabile in initiation of replication from the chromosomal origin of Escherichia coli
Department of Biochemistry, Michigan State University, East Lansing 48824-1319.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  M. F. Susin, R. L. Baldini, F. Gueiros-Filho, and S. L. Gomes GroES/GroEL and DnaK/DnaJ Have Distinct Roles in Stress Responses and during Cell Cycle Progression in Caulobacter crescentus J. Bacteriol., December 1, 2006; 188(23): 8044 - 8053. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y. Masuda, R. A. O. Bennett, and B. Demple Dynamics of the Interaction of Human Apurinic Endonuclease (Ape1) with Its Substrate and Product J. Biol. Chem., November 13, 1998; 273(46): 30352 - 30359. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Hase, T. Yoshimi, Y. Ishikawa, A. Ohba, L. Guo, S. Mima, M. Makise, Y. Yamaguchi, T. Tsuchiya, and T. Mizushima Site-directed Mutational Analysis for the Membrane Binding of DnaA Protein. IDENTIFICATION OF AMINO ACIDS INVOLVED IN THE FUNCTIONAL INTERACTION BETWEEN DnaA PROTEIN AND ACIDIC PHOSPHOLIPIDS J. Biol. Chem., October 30, 1998; 273(44): 28651 - 28656. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Mizushima, T. Takaki, T. Kubota, T. Tsuchiya, T. Miki, T. Katayama, and K. Sekimizu Site-directed Mutational Analysis for the ATP Binding of DnaA Protein. FUNCTIONS OF TWO CONSERVED AMINO ACIDS (LYS-178 AND ASP-235) LOCATED IN THE ATP-BINDING DOMAIN OF DnaA PROTEIN IN VITRO AND IN VIVO J. Biol. Chem., August 14, 1998; 273(33): 20847 - 20851. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Marszalek, W. Zhang, T. R. Hupp, C. Margulies, K. M. Carr, S. Cherry, and J. M. Kaguni Domains of DnaA Protein Involved in Interaction with DnaB Protein, and in Unwinding the Escherichia coli Chromosomal Origin J. Biol. Chem., August 2, 1996; 271(31): 18535 - 18542. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Garwood and M. Kohiyama A Novel Cytoplasmic Hemimethylated oriC Binding Activity J. Biol. Chem., March 29, 1996; 271(13): 7404 - 7411. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
B. Banecki, A. Wawrzynow, J. Puzewicz, C. Georgopoulos, and M. Zylicz Structure-Function Analysis of the Zinc-binding Region of the ClpX Molecular Chaperone J. Biol. Chem., May 25, 2001; 276(22): 18843 - 18848. [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 |
