Interactions of Nucleotide Cofactors with theEscherichia coliReplication Factor DnaC Protein†

Biochemistry ◽  
2000 ◽  
Vol 39 (42) ◽  
pp. 12959-12969 ◽  
Author(s):  
Roberto Galletto ◽  
Surendran Rajendran ◽  
Wlodzimierz Bujalowski
Keyword(s):  
Dnac Protein

The Nucleotide-Binding Site of the Escherichia coli DnaC Protein: Molecular Topography of DnaC Protein–Nucleotide Cofactor Complexes

2005 ◽  
Vol 43 (3) ◽  
pp. 331-354 ◽  
Author(s):  
Roberto Galletto ◽  
Maria J. Jezewska ◽  
Rodrigo Maillard ◽  
Wlodzimierz Bujalowski
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Nucleotide Binding ◽  
Nucleotide Binding Site ◽  
Dnac Protein

Global Conformation of theEscherichia coliReplication Factor DnaC Protein in Absence and Presence of Nucleotide Cofactors†

Biochemistry ◽  
2004 ◽  
Vol 43 (34) ◽  
pp. 10988-11001 ◽  
Author(s):  
Roberto Galletto ◽  
Rodrigo Maillard ◽  
Maria J. Jezewska ◽  
Wlodzimierz Bujalowski
Keyword(s):  
Dnac Protein

scholarly journals Escherichia coliDnaB Helicase−DnaC Protein Complex: Allosteric Effects of the Nucleotides on the Nucleic Acid Binding and the Kinetic Mechanism of NTP Hydrolysis. 3

Biochemistry ◽  
2009 ◽  
Vol 48 (29) ◽  
pp. 6747-6763 ◽  
Author(s):  
Anasuya Roychowdhury ◽  
Michal R. Szymanski ◽  
Maria J. Jezewska ◽  
Wlodzimierz Bujalowski
Keyword(s):  
Nucleic Acid ◽  
Protein Complex ◽  
Kinetic Mechanism ◽  
Nucleic Acid Binding ◽  
Dnac Protein

scholarly journals Interactions of theEscherichia coliDnaB−DnaC Protein Complex with Nucleotide Cofactors. 1. Allosteric Conformational Transitions of the Complex

Biochemistry ◽  
2009 ◽  
Vol 48 (29) ◽  
pp. 6712-6729 ◽  
Author(s):  
Anasuya Roychowdhury ◽  
Michal R. Szymanski ◽  
Maria J. Jezewska ◽  
Wlodzimierz Bujalowski
Keyword(s):  
Protein Complex ◽  
Conformational Transitions ◽  
Dnac Protein

scholarly journals Quantitative analysis of nucleotide modulation of DNA binding by DnaC protein of Escherichia coli

2004 ◽  
Vol 379 (3) ◽  
pp. 553-562 ◽  
Author(s):  
Subhasis B. BISWAS ◽  
Stephen FLOWERS ◽  
Esther E. BISWAS-FISS
Keyword(s):  
Escherichia Coli ◽  
Quantitative Analysis ◽  
Dna Replication ◽  
Dna Binding ◽  
Binding Affinity ◽  
Replication Fork ◽  
Dna Helicase ◽  
Replication Initiation ◽  
Chromosomal Dna ◽  
Dnac Protein

In this study, we have presented the first report of Escherichia coli DnaC protein binding to ssDNA (single stranded DNA) in an apparent hexameric form. DnaC protein transfers DnaB helicase onto a nascent chromosomal DNA replication fork at oriC, the origin of E. coli DNA replication. In eukaryotes, Cdc6 protein may play a similar role in the DNA helicase loading in the replication fork during replication initiation at the origin. We have analysed the DNA-binding properties of DnaC protein and a quantitative analysis of the nucleotide regulation of DnaC–DNA and DnaC–DnaB interactions using fluorescence anisotropy and affinity sensor analysis. DnaC protein bound to ssDNA with low to moderate affinity and the affinity was strictly modulated by nucleotides. DnaC bound ssDNA in the complete absence of nucleotides. The DNA-binding affinity was significantly increased in the presence of ATP, but not ATP[S]. In the presence of ADP, the binding affinity decreased approximately fifty-fold. Both anisotropy and biosensor analyses demonstrated that with DnaC protein, ATP facilitated ssDNA binding, whereas ADP facilitated its dissociation from ssDNA, which is a characteristic of an ATP/ADP switch. Both ssDNA and nucleotides modulate DnaB6•DnaC6 complex formation, which has significant implications in DnaC protein function. Based on the thermodynamic data provided in this study, we have proposed a mechanism of DnaB loading on to ssDNA by DnaC protein.

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