Structural Characteristics of the Nucleotide-Binding Site of Escherichia coli Primary Replicative Helicase DnaB Protein. Studies with Ribose and Base-Modified Fluorescent Nucleotide Analogs

Biochemistry ◽  
1994 ◽  
Vol 33 (15) ◽  
pp. 4682-4694 ◽  
Author(s):  
Wlodzimierz Bujalowski ◽  
Malgorzata Maria Klonowska
2005 ◽  
Vol 43 (3) ◽  
pp. 331-354 ◽  
Author(s):  
Roberto Galletto ◽  
Maria J. Jezewska ◽  
Rodrigo Maillard ◽  
Wlodzimierz Bujalowski

1986 ◽  
Vol 5 (6) ◽  
pp. 1351-1358 ◽  
Author(s):  
J. Tucker ◽  
G. Sczakiel ◽  
J. Feuerstein ◽  
J. John ◽  
R.S. Goody ◽  
...  

2000 ◽  
Vol 182 (14) ◽  
pp. 4124-4127 ◽  
Author(s):  
David S. Boyle ◽  
Dawn Grant ◽  
G. Craig Draper ◽  
William D. Donachie

ABSTRACT Resolution of chromosome dimers, by site-specific recombination between dif sites, is carried out in Escherichia coli by XerCD recombinase in association with the FtsK protein. We show here that a variety of altered FtsK polypeptides, consisting of the N-terminal (cell division) domain alone or with deletions in the proline-glutamine-rich part of the protein, or polypeptides consisting of the C-terminal domain alone are all unable to carry outdif recombination. Alteration of the putative nucleotide-binding site also abolishes the ability of FtsK to carry out recombination between dif sites.


2008 ◽  
Vol 470 (1) ◽  
pp. 20-26 ◽  
Author(s):  
Majbritt Thymark ◽  
Eva Johansson ◽  
Sine Larsen ◽  
Martin Willemoës

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