Cooperativity: Action at a distance in a classic system

Current Biology

Volumn 10, Issue 19, 2000, Pages

  Koudelka, Gerald B ^a  

^a UNIVERSITY AT BUFFALO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOPHAGE LAMBDA;

EID: 0034609736     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(00)00710-7     Document Type: Review

References (12)

1. Interaction at a distance between lambda repressors disrupts gene activation
2. Structure of the λ complex at 2.5 Å resolution: Details of the repressor-operator interaction
3. Crystal structure of the lambda repressor C-terminal domain provides a model for cooperative operator binding
4. Autodigestion of lexA and phage λ repressors
5. Homology among DNA-binding proteins suggests use of a conserved supersecondary structure
6. Structure of the UmuD' protein and its regulation in response to DNA damage
7. Mutations affecting the ability of the Escherichia coli UmuD' protein to participate in SOS mutagenesis
8. Expression, purification, and functional characterization of the carboxyl-terminal domain fragment of bacteriophage 434 repressor
9. The structure of the E. coli recA protein monomer and polymer
10. Four dimers of lambda repressor bound to two suitably spaced pairs of lambda operators form octamers and DNA loops over large distances
11. Linkage between operator binding and dimer to octamer self-assembly of bacteriophage λ cl repressor