Negative cooperativity in the binding of nucleotides to Escherichia coli replicative helicase DnaB protein. Interactions with fluorescent nucleotide analogs

Biochemistry ◽  
1993 ◽  
Vol 32 (22) ◽  
pp. 5888-5900 ◽  
Author(s):  
Wlodzimierz Bujalowski ◽  
Malgorzata Maria Klonowska
Keyword(s):  
Escherichia Coli ◽  
Protein Interactions ◽  
Negative Cooperativity ◽  
Nucleotide Analogs ◽  
Replicative Helicase ◽  
Helicase Dnab

scholarly journals Initiation of Heat-Induced Replication Requires DnaA and the L-13-mer of oriC

2006 ◽  
Vol 188 (23) ◽  
pp. 8294-8298 ◽  
Author(s):  
Rocío González-Soltero ◽  
Emilia Botello ◽  
Alfonso Jiménez-Sánchez
Keyword(s):  
Escherichia Coli ◽  
Growth Temperature ◽  
Binding Sites ◽  
Functional Requirements ◽  
Bacterial Strains ◽  
Replicative Helicase ◽  
Helicase Dnab ◽  
Duplex Destabilization ◽  
Theoretical Stress ◽  
L 13

ABSTRACT An upshift of 10°C or more in the growth temperature of an Escherichia coli culture causes induction of extra rounds of chromosome replication. This stress replication initiates at oriC but has functional requirements different from those of cyclic replication. We named this phenomenon h eat- i nduced r eplication (HIR). Analysis of HIR in bacterial strains that had complete or partial oriC deletions and were suppressed by F integration showed that no sequence outside oriC is used for HIR. Analysis of a number of oriC mutants showed that deletion of the L-13-mer, which makes oriC inactive for cyclic replication, was the only mutation studied that inactivated HIR. The requirement for this sequence was strictly correlated with Benham's theoretical stress-induced DNA duplex destabilization. oriC mutations at DnaA, FIS, or IHF binding sites showed normal HIR activation, but DnaA was required for HIR. We suggest that strand opening for HIR initiation occurs due to heat-induced destabilization of the L-13-mer, and the stable oligomeric DnaA-single-stranded oriC complex might be required only to load the replicative helicase DnaB.

scholarly journals The Protein Interactome of Glycolysis in Escherichia coli

Proteomes ◽  
2021 ◽  
Vol 9 (2) ◽  
pp. 16
Author(s):  
Shomeek Chowdhury ◽  
Stephen Hepper ◽  
Mudassir K. Lodi ◽  
Milton H. Saier ◽  
Peter Uetz
Keyword(s):  
Escherichia Coli ◽  
Protein Interactions ◽  
Allosteric Regulation ◽  
Glycolytic Enzymes ◽  
Protein Protein Interactions ◽  
Post Translational Modification ◽  
Interacting Protein ◽  
E Coli ◽  
Protein Interactome ◽  
The Impact

Glycolysis is regulated by numerous mechanisms including allosteric regulation, post-translational modification or protein-protein interactions (PPI). While glycolytic enzymes have been found to interact with hundreds of proteins, the impact of only some of these PPIs on glycolysis is well understood. Here we investigate which of these interactions may affect glycolysis in E. coli and possibly across numerous other bacteria, based on the stoichiometry of interacting protein pairs (from proteomic studies) and their conservation across bacteria. We present a list of 339 protein-protein interactions involving glycolytic enzymes but predict that ~70% of glycolytic interactors are not present in adequate amounts to have a significant impact on glycolysis. Finally, we identify a conserved but uncharacterized subset of interactions that are likely to affect glycolysis and deserve further study.

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