Identification of the RecA protein-loading domain of RecBCD enzyme

Journal of Molecular Biology

Volumn 297, Issue 3, 2000, Pages 537-542

  Churchill, Jason J ^a   Kowalczykowski, Stephen C ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Chi sequence; Helicase; RecA protein; RecBCD enzyme; Recombination

Indexed keywords

CELL DNA; PROTEIN RECBCD; RECA PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; DNA RECOMBINATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SUBUNIT; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA INTERACTION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION;

ESCHERICHIA COLI;

EID: 0034737310     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3590     Document Type: Article

References (24)

1. The recombination hot spot χ is a regulatory element that switches the polarity of DNA degradation by the RecBCD enzyme
2. The translocating RecBCD enzyme stimulates recombination by directing RecA protein onto ssDNA in a χ-regulated manner
3. A single mutation, RecB(D1080A), eliminates RecA protein loading but not Chi recognition by RecBCD enzyme
4. Facilitated loading of RecA protein is essential to recombination by RecBCD enzyme
5. The RecBC enzyme loads RecA protein onto ssDNA asymmetrically and independently of χ, resulting in constitutive recombination activation
6. Recombination and UV resistance of Escherichia coli with the cloned recA and recBCD genes of Serratia marcescens and Proteus mirabilis: Evidence for an advantage of intraspecies combination of P. mirabilis RecA protein and RecBCD enzyme
7. Homologous pairing in vitro stimulated by the recombination hotspot, Chi
8. The recombination hotspot χ is a regulatory sequence that acts by attenuating the nuclease activity of the E. coli RecBCD enzyme
9. RecA protein rapidly crystallizes in the presence of spermidine: A valuable step in its purification and physical characterization
10. Molecular amplification and purification of the E. coli recC gene product
11. Biochemical and biological function of Escherichia coli RecA protein: Behavior of mutant RecA proteins
12. Effects of the Escherichia coli SSB protein on the single-stranded DNA-dependent ATPase activity of Escherichia coli RecA protein: Evidence that SSB protein facilitates the binding of RecA protein to regions of secondary structure within single-stranded DNA
13. Effects of the Escherichia coli SSB protein on the binding of Escherichia coli RecA protein to single-stranded DNA: Demonstration of competitive binding and the lack of a specific protein-protein interaction
14. Collapse and repair of replication forks in Escherichia coli
15. Staying on track: Common features of DNA helicases and microtubule motors
16. DNA double-strand breaks caused by replication arrest
17. The recA-recBCD dependent recombination pathways of Serratia marcescens and Proteus mirabilis in Escherichia coli: Functions of hybrid enzymes and hybrid pathways
18. Formation of heteroduplex DNA promoted by the combined activities of Escherichia coli RecA and RecBCD proteins
19. Substrate specificity of the DNA unwinding activity of the RecBC enzyme of Escherichia coli
20. The 30-kDa C-terminal domain of the RecB protein is critical for the nuclease activity, but not the helicase activity, of the RecBCD enzyme from Escherichia coli
21. Identification of the nuclease active site in the multifunctional RecBCD enzyme by creation of a chimeric enzyme