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Journal of Virology, August 2001, p. 7206-7209, Vol. 75, No. 15
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.15.7206-7209.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

DNA and ATP Binding Activities of the Baculovirus DNA Helicase P143

Vivien V. McDougal1 and Linda A. Guarino1,2,*

Departments of Biochemistry and Biophysics1 and Entomology,2 Texas A&M University, College Station, Texas 77843-2128

Received 26 February 2001/Accepted 2 May 2001

P143 is a DNA helicase that tightly binds both double-stranded and single-stranded DNA. DNA-protein complexes rapidly dissociated in the presence of ATP and Mg2+. This finding suggests that ATP hydrolysis causes a conformational change in P143 which decreases affinity for DNA. This supports the model of an inchworm mechanism of DNA unwinding.

* Corresponding author. Mailing address: Department of Biochemistry and Biophysics, Texas A&M University, MS2128, College Station, TX 77843-2128. Phone: (409) 845-7556. Fax: (409) 845-9274. E-mail: lguarino{at}tamu.edu.

Journal of Virology, August 2001, p. 7206-7209, Vol. 75, No. 15
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.15.7206-7209.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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