ADP-mediated dissociation of stable complexes of recA protein and single-stranded DNA.

M. M. Cox, D. A. Soltis, I. R. Lehman, C. DeBrosse, S. J. Benkovic

Research output: Contribution to journalArticle

44 Citations (Scopus)

Abstract

The complete exchange of strands between circular single-stranded and full length linear duplex DNAs promoted by the recA protein of Escherichia coli is dependent upon the hydrolysis of ATP and is strongly stimulated by the single-stranded DNA binding protein (SSB). In the presence of SSB, stable complexes of recA protein and single-stranded DNA are formed as an early step in the reaction. These complexes dissociate when the ADP/ATP ratio approaches a value of 0.6-1.5, depending upon reaction conditions. Thus, ATP hydrolysis never proceeds to completion but stops when 40-60% of the input ATP has undergone hydrolysis. recA protein can participate in a second round of strand exchange upon regeneration of the ATP. While 100-200 mol of ATP are hydrolyzed/mol of heteroduplex base pair formed under standard reaction conditions in the presence of SSB, this value is reduced to 16 at levels of ADP lower than that required to dissociate the complexes. ATP hydrolysis appears to be completely irreversible since efforts to detect exchange reactions using 18O probes have been unsuccessful.

Original languageEnglish (US)
Pages (from-to)2586-2592
Number of pages7
JournalJournal of Biological Chemistry
Volume258
Issue number4
StatePublished - Feb 25 1983

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Rec A Recombinases
Single-Stranded DNA
Adenosine Diphosphate
Adenosine Triphosphate
Hydrolysis
DNA-Binding Proteins
Base Pairing
Escherichia coli
Regeneration
DNA

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Cox, M. M., Soltis, D. A., Lehman, I. R., DeBrosse, C., & Benkovic, S. J. (1983). ADP-mediated dissociation of stable complexes of recA protein and single-stranded DNA. Journal of Biological Chemistry, 258(4), 2586-2592.
Cox, M. M. ; Soltis, D. A. ; Lehman, I. R. ; DeBrosse, C. ; Benkovic, S. J. / ADP-mediated dissociation of stable complexes of recA protein and single-stranded DNA. In: Journal of Biological Chemistry. 1983 ; Vol. 258, No. 4. pp. 2586-2592.
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abstract = "The complete exchange of strands between circular single-stranded and full length linear duplex DNAs promoted by the recA protein of Escherichia coli is dependent upon the hydrolysis of ATP and is strongly stimulated by the single-stranded DNA binding protein (SSB). In the presence of SSB, stable complexes of recA protein and single-stranded DNA are formed as an early step in the reaction. These complexes dissociate when the ADP/ATP ratio approaches a value of 0.6-1.5, depending upon reaction conditions. Thus, ATP hydrolysis never proceeds to completion but stops when 40-60{\%} of the input ATP has undergone hydrolysis. recA protein can participate in a second round of strand exchange upon regeneration of the ATP. While 100-200 mol of ATP are hydrolyzed/mol of heteroduplex base pair formed under standard reaction conditions in the presence of SSB, this value is reduced to 16 at levels of ADP lower than that required to dissociate the complexes. ATP hydrolysis appears to be completely irreversible since efforts to detect exchange reactions using 18O probes have been unsuccessful.",
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Cox, MM, Soltis, DA, Lehman, IR, DeBrosse, C & Benkovic, SJ 1983, 'ADP-mediated dissociation of stable complexes of recA protein and single-stranded DNA.', Journal of Biological Chemistry, vol. 258, no. 4, pp. 2586-2592.

ADP-mediated dissociation of stable complexes of recA protein and single-stranded DNA. / Cox, M. M.; Soltis, D. A.; Lehman, I. R.; DeBrosse, C.; Benkovic, S. J.

In: Journal of Biological Chemistry, Vol. 258, No. 4, 25.02.1983, p. 2586-2592.

Research output: Contribution to journalArticle

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AU - Soltis, D. A.

AU - Lehman, I. R.

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AU - Benkovic, S. J.

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N2 - The complete exchange of strands between circular single-stranded and full length linear duplex DNAs promoted by the recA protein of Escherichia coli is dependent upon the hydrolysis of ATP and is strongly stimulated by the single-stranded DNA binding protein (SSB). In the presence of SSB, stable complexes of recA protein and single-stranded DNA are formed as an early step in the reaction. These complexes dissociate when the ADP/ATP ratio approaches a value of 0.6-1.5, depending upon reaction conditions. Thus, ATP hydrolysis never proceeds to completion but stops when 40-60% of the input ATP has undergone hydrolysis. recA protein can participate in a second round of strand exchange upon regeneration of the ATP. While 100-200 mol of ATP are hydrolyzed/mol of heteroduplex base pair formed under standard reaction conditions in the presence of SSB, this value is reduced to 16 at levels of ADP lower than that required to dissociate the complexes. ATP hydrolysis appears to be completely irreversible since efforts to detect exchange reactions using 18O probes have been unsuccessful.

AB - The complete exchange of strands between circular single-stranded and full length linear duplex DNAs promoted by the recA protein of Escherichia coli is dependent upon the hydrolysis of ATP and is strongly stimulated by the single-stranded DNA binding protein (SSB). In the presence of SSB, stable complexes of recA protein and single-stranded DNA are formed as an early step in the reaction. These complexes dissociate when the ADP/ATP ratio approaches a value of 0.6-1.5, depending upon reaction conditions. Thus, ATP hydrolysis never proceeds to completion but stops when 40-60% of the input ATP has undergone hydrolysis. recA protein can participate in a second round of strand exchange upon regeneration of the ATP. While 100-200 mol of ATP are hydrolyzed/mol of heteroduplex base pair formed under standard reaction conditions in the presence of SSB, this value is reduced to 16 at levels of ADP lower than that required to dissociate the complexes. ATP hydrolysis appears to be completely irreversible since efforts to detect exchange reactions using 18O probes have been unsuccessful.

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Cox MM, Soltis DA, Lehman IR, DeBrosse C, Benkovic SJ. ADP-mediated dissociation of stable complexes of recA protein and single-stranded DNA. Journal of Biological Chemistry. 1983 Feb 25;258(4):2586-2592.