Literature DB >> 6251042

Enzyme-catalyzed DNA unwinding. The role of ATP in helicase III activity.

R H Das, G T Yarranton, M L Gefter.   

Abstract

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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Year:  1980        PMID: 6251042

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  2 in total

Review 1.  Biochemistry of homologous recombination in Escherichia coli.

Authors:  S C Kowalczykowski; D A Dixon; A K Eggleston; S D Lauder; W M Rehrauer
Journal:  Microbiol Rev       Date:  1994-09

2.  Theoretical aspects of translocation on DNA: adenosine triphosphatases and treadmilling binding proteins.

Authors:  T L Hill; T Tsuchiya
Journal:  Proc Natl Acad Sci U S A       Date:  1981-08       Impact factor: 11.205

  2 in total

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