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  Bridwell and DeWald's Textbook of Spinal Surgery : Editors in Chief, Munish C. Gupta, Keith H. Bridwell ; Associate Editors, Paul a. Anderson [and 13 Others]. Fourth edition

  Bridwell, Keith H.; Dewald, Ronald L.; Gupta, Munish C.

  Digital Access LWW Health Library 2020
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• Article

  Ionic strength perturbation kinetics of gene 32 protein dissociation from its complex with single-stranded DNA.

  Peterman BF, Wu CW.

  Biochemistry. 1978 Sep 05;17(18):3889-92.

  Equilibrium and kinetic studies of the interaction of gene 32 protein of T4 phage with single-stranded fd DNA were performed monitoring the changes in protein fluorescence. From the fluorescence titrations, it was estimated that a monomer of gene 32 protein covered six nucleotide bases on the DNA and the lower limit for the apparent association constant was 1.9 x 10(8) M-1 with a cooperative parameter of 10(3) in 0.1 M 2-amino-2-hydroxymethyl-1,3-propanediol hydrochloride (pH 7) at 25 degrees C. When an ionic strength jump was applied to the gene 32 protein-fd DNA complex using a stopped-flow apparatus, the complex underwent a dissociation into its individual components accompanied by an increase in protein fluorescence. The kinetics of the dissociation are not consistent with a single first-order process. The data, however, can be analyzed in terms of a model in which gene 32 protein molecules release cooperatively starting from either one or both ends of a cluster of proteins bound to fd DNA. This type of dissociation of gene 32 protein from single-stranded DNA is very efficient and has interesting implications: it could provide a way to facilitate a rapid "zippering" of the two complementary DNA strands during DNA replication and genetic recombination.

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