Enzyme-catalyzed DNA unwinding. The role of ATP in helicase III activity
The enzyme helicase III catalyzes ATP-dependent unwinding of double-stranded DNA (Yarranto, G. T., Das, R. H., and Gefter, M. L. (1979) J. Biol. Chem. 254, 11997-12001). The free enzyme is able to bind to double- and single-stranded DNA. In the presence of ATP the enzyme can bind single- but not dou...
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Veröffentlicht in: | The Journal of biological chemistry 1980-09, Vol.255 (17), p.8069-8073 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The enzyme helicase III catalyzes ATP-dependent unwinding of double-stranded DNA (Yarranto, G. T., Das, R. H., and Gefter,
M. L. (1979) J. Biol. Chem. 254, 11997-12001). The free enzyme is able to bind to double- and single-stranded DNA. In the
presence of ATP the enzyme can bind single- but not double-stranded DNA. The enzyme catalyzes an ADP-ATP exchange reaction
in the absence of DNA. It is suggested that there is an enzyme.phosphate complex that discriminates between the two forms
of DNA. These results are discussed in relation to a model that accounts for catalytic unwinding of DNA coupled to ATP hydrolysis. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(19)70608-5 |