Multiple-step kinetic mechanism of DNA-independent ATP binding and hydrolysis by Escherichia coli replicative helicase DnaB protein: quantitative analysis using the rapid quench-flow method 1 1Edited by D. Draper

2000 ◽  
Vol 303 (5) ◽  
pp. 773-795 ◽  
Author(s):  
Surendran Rajendran ◽  
Maria J. Jezewska ◽  
Wlodzimierz Bujalowski
Keyword(s):  
Escherichia Coli ◽  
Quantitative Analysis ◽  
Kinetic Mechanism ◽  
Atp Binding ◽  
Replicative Helicase ◽  
Flow Method ◽  
Rapid Quench ◽  
Helicase Dnab ◽  
Atp Binding And Hydrolysis ◽  
Multiple Step

scholarly journals Origin Licensing Requires ATP Binding and Hydrolysis by the MCM Replicative Helicase

2014 ◽  
Vol 55 (5) ◽  
pp. 666-677 ◽  
Author(s):  
Gideon Coster ◽  
Jordi Frigola ◽  
Fabienne Beuron ◽  
Edward P. Morris ◽  
John F.X. Diffley
Keyword(s):  
Atp Binding ◽  
Replicative Helicase ◽  
Origin Licensing ◽  
Atp Binding And Hydrolysis

scholarly journals Structural and Biochemical Studies on ATP Binding and Hydrolysis by the Escherichia coli RNA Chaperone Hfq

PLoS ONE ◽  
2012 ◽  
Vol 7 (11) ◽  
pp. e50892 ◽  
Author(s):  
Hermann Hämmerle ◽  
Mads Beich-Frandsen ◽  
Branislav Večerek ◽  
Lukas Rajkowitsch ◽  
Oliviero Carugo ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Atp Binding ◽  
Rna Chaperone ◽  
Biochemical Studies ◽  
Atp Binding And Hydrolysis

scholarly journals Asymmetric MukB ATPases are regulated independently by the N- and C-terminal domains of MukF kleisin

2017 ◽  
Author(s):  
Katarzyna Zawadzka ◽  
Pawel Zawadzki ◽  
Rachel Baker ◽  
Karthik V. Rajasekar ◽  
David J. Sherratt ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Chromosome Segregation ◽  
Active Sites ◽  
Atp Binding ◽  
Dimerization Domain ◽  
Helix Bundle ◽  
Terminal Domain ◽  
Atp Binding And Hydrolysis ◽  
Terminal Domains

AbstractThe Escherichia coli SMC complex, MukBEF, acts in chromosome segregation. MukBEF shares the distinctive architecture of other SMC complexes, with one prominent difference; unlike other kleisins, MukF forms dimers through its N-terminal domain. We show that a 4-helix bundle adjacent to the MukF dimerization domain interacts functionally with the MukB coiled-coiled ‘neck’ adjacent to the ATPase head, forming an asymmetric tripartite complex, as in other SMC complexes. Since MukF dimerization is preserved during this interaction, MukF directs the formation of dimer of dimers MukBEF complexes, observed previously in vivo. The MukF N- and C-terminal domains stimulate ATPase independently and additively, consistent with them each targeting only one of the two MukB ATPase active sites in the asymmetric complex. We demonstrate that MukF interaction with the MukB neck turns over during cycles of ATP binding and hydrolysis in vivo and that impairment of this interaction leads to MukBEF release from chromosomes.

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