Synergy between the N-terminal and C-terminal domains of Mycobacterium tuberculosis HupB is essential for high-affinity binding, DNA supercoiling and inhibition of RecA-promoted strand exchange.

Sharadamma, N

Synergy between the N-terminal and C-terminal domains of Mycobacterium tuberculosis HupB is essential for high-affinity binding, DNA supercoiling and inhibition of RecA-promoted strand exchange. [electronic resource] - The FEBS journal Sep 2011 - 3447-62 p. digital

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

1742-4658

10.1111/j.1742-4658.2011.08267.x doi


Bacterial Proteins--chemistry
Carrier Proteins--chemistry
Cross-Linking Reagents--chemistry
DNA, Bacterial--chemistry
DNA, Superhelical--chemistry
DNA-Binding Proteins--chemistry
Dimerization
Escherichia coli--metabolism
Escherichia coli Proteins--chemistry
Histones--chemistry
Kinetics
Mutant Proteins--chemistry
Mycobacterium tuberculosis--metabolism
Peptide Fragments--chemistry
Polydeoxyribonucleotides--chemistry
Protein Interaction Domains and Motifs
Protein Stability
Rec A Recombinases--antagonists & inhibitors
Recombinant Proteins--chemistry
Recombination, Genetic
Transcription Factors--chemistry