+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Hydrolysis of ATP dependent on homologous double-stranded DNA and single-stranded fragments promoted by RecA protein of Escherichia coli



Hydrolysis of ATP dependent on homologous double-stranded DNA and single-stranded fragments promoted by RecA protein of Escherichia coli



Journal of Biochemistry 91(5): 1767-1775



RecA protein is essential to general genetic recombination in Escherichia coli. In the presence of ATP, a stoichiometric amount of recA protein forms D-loops from superhelical closed-circular DNA (form I DNA) and homologous single-stranded fragments, and subsequently dissociates the D-loops. Under appropriate conditions, the hydrolysis of ATP by recA protein depends on the presence of both double-stranded DNA and homologous single-stranded fragments (homology-dependent hydrolysis). In the presence of form I DNA, most of the homology-dependent hydrolysis of ATP by recA protein is related to the dissociation of D-loops rather than the formation of D-loops. RecA protein also promoted the homology-dependent hydrolysis of ATP in the presence of nicked-circular DNA (form II DNA), but unlike the case of form I DNA, this hydrolysis was associated with an increase in the amount of mature D-loops that were detected by the D-loop assay. When double-stranded DNA was superhelical, the homology-dependent hydrolysis of ATP continued at the same rate even after all the D-loops were dissociated. This correlates with our earlier observation that in the process of formation and dissociation of D-loops, form I DNA was converted to an inactive substrate without any apparent damage to the DNA, probably by the formation of a complex with recA protein. All of the observations described above can be explained by a model in which a common mechanism causes dissociation of D-loops from form I DNA, inactivation of form I DNA, and growth of D-loops in form II DNA. The mechanism might involve cooperative binding of recA protein to the duplex DNA from the site of the nascent D-loop, resulting in unidirectional unwinding of the duplex DNA.

Please choose payment method:






(PDF emailed within 1 workday: $29.90)

Accession: 043296162

Download citation: RISBibTeXText

PMID: 7047518


Related references

Hydrolysis of Atp Dependent on Homologous Double-Stranded Dna and Single-Stranded Fragments Promoted by RecA Protein of Escherichia coli11. The Journal of Biochemistry 91(5): 1767-1775, 1982

Effects of 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. Journal of Molecular Biology 193(1): 97-114, 1987

Homologous pairing of single-stranded DNA and superhelical double-stranded DNA catalyzed by RecO protein from Escherichia coli. Journal of Bacteriology 177(3): 566-572, 1995

On the mechanism of pairing of single- and double-stranded DNA molecules by the recA and single-stranded DNA-binding proteins of Escherichia coli. Journal of Biological Chemistry 261(3): 1025-1030, 1986

DNA strand exchange promoted by recA protein and single-stranded DNA-binding protein of Escherichia coli. Cold Spring Harbor Symposia on Quantitative Biology 47 Pt 2: 803-810, 1983

recA protein-promoted DNA strand exchange. Stable complexes of recA protein and single-stranded DNA formed in the presence of ATP and single-stranded DNA binding protein. Journal of Biological Chemistry 257(14): 8523-8532, 1982

Binding of the recA protein of Escherichia coli to single- and double-stranded DNA. Journal of Biological Chemistry 256(16): 8835-8844, 1981

Continuous association of Escherichia coli single-stranded DNA binding protein with stable complexes of recA protein and single-stranded DNA. Biochemistry 25(7): 1482-1494, 1986

Reversibility of strand invasion promoted by recA protein and its inhibition by Escherichia coli single-stranded DNA-binding protein or phage T4 gene 32 protein. Journal of Biological Chemistry 263(1): 200-209, 1988

Purified escherichia coli reca protein catalyzes homoeologous pairing of super helical dna and single stranded fragments. Proceedings of the National Academy of Sciences of the United States of America 76(4): 1638-1642, 1979

Recognition and alignment of homologous DNA sequences between minichromosomes and single-stranded DNA promoted by RecA protein. Molecular & General Genetics 249(3): 336-348, 1995

Direct evidence of the role of ATPγS in the binding of single-stranded binding protein (Escherichia coli) and RecA to single-stranded DNA. Langmuir 26(18): 14755-8, 2011

RecA protein promoted homologous pairing in vitro. Pairing between linear duplex DNA bound to HU Protein (nucleosome cores) and nucleoprotein filaments of recA protein-single-stranded DNA. Journal of Biological Chemistry 264(29): 17395-17400, 1989

Homologous recognition and triplex formation promoted by RecA protein between duplex oligonucleotides and single-stranded DNA. Journal of Molecular Biology 229(2): 328-343, 1993

Effects of overproduction of single stranded dna binding protein on reca protein dependent processes in escherichia coli. Journal of Cellular Biochemistry Suppl. (12 PART A): 345, 1988