Spectroscopic studies of the nucleotide binding site of elongation factor Tu from Escherichia coli. An approach to characterizing the elementary steps of the elongation cycle of protein biosynthesis

Biochemistry ◽  
1981 ◽  
Vol 20 (21) ◽  
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1987 ◽  
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pp. 9263-9277 ◽  
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Marcus Peter ◽  
Franz Meissner ◽  
Mathias Sprinzl

2005 ◽  
Vol 43 (3) ◽  
pp. 331-354 ◽  
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Maria J. Jezewska ◽  
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Wlodzimierz Bujalowski

Biochemistry ◽  
2000 ◽  
Vol 39 (44) ◽  
pp. 13558-13564 ◽  
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Philippe Gonzalo ◽  
Bruno Sontag ◽  
Jean-Pierre Lavergne ◽  
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Jean-Paul Reboud

1986 ◽  
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FEBS Letters ◽  
1979 ◽  
Vol 98 (2) ◽  
pp. 329-332 ◽  
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Jiří Smrt ◽  
Antonín Holý

2000 ◽  
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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.


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