Kinetic modeling of the RecA protein promoted renaturation of complementary DNA strands

Floyd Ransom Bryant, K. L. Menge, T. T. Nguyen

Research output: Contribution to journalArticle

Abstract

Quantitative agarose gel assays reveal that the recA protein promoted renaturation of complementary DNA strands (φX DNA) proceeds in two stages. The first stage results in the formation of unit-length duplex DNA as well as a distribution of other products ("initial products"). In the second stage, the initial products are converted to complex multipaired DNA structures ("network DNA"). In the presence of ATP, the initial products are formed within 2 min and are then rapidly converted to network DNA. In the absence of ATP, the initial products are formed nearly as fast as with ATP present, but they are converted to network DNA at a much lower rate. The time-dependent formation of initial products and network DNA from complementary single strands for both the ATP-stimulated and ATP-independent reactions can be modeled by using a simple two-step sequential kinetic scheme. This model indicates that the primary effect of ATP in the recA protein promoted renaturation reaction is not on the initial pairing step (which leads to the formation of initial products) but rather is to increase the rate at which subsequent pairing events can occur.

Original languageEnglish (US)
Pages (from-to)1062-1069
Number of pages8
JournalBiochemistry®
Volume28
Issue number3
StatePublished - 1989

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Protein Renaturation
Rec A Recombinases
Complementary DNA
Adenosine Triphosphate
Kinetics
DNA
Sepharose
Assays
Gels

ASJC Scopus subject areas

  • Biochemistry

Cite this

Kinetic modeling of the RecA protein promoted renaturation of complementary DNA strands. / Bryant, Floyd Ransom; Menge, K. L.; Nguyen, T. T.

In: Biochemistry®, Vol. 28, No. 3, 1989, p. 1062-1069.

Research output: Contribution to journalArticle

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