Sakakibara, N.
, Schwarz, F.
and Kelman, Z.
(2009),
ATP hydrolysis and DNA binding confer thermostability on the MCM helicase, ACS Biochemistry, [online], https://doi.org/10.1021/bi801921, https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=832435
(Accessed August 8, 2025)
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ATP hydrolysis and DNA binding confer thermostability on the MCM helicase
Published
Author(s)
Nozomi Sakakibara, ,
Abstract
Minichromosome maintenance (MCM) helicase is the replicative helicase in archaea. The enzyme utilizes the energy derived from ATP hydrolysis to translocate along one strand of the DNA and unwind the complementary strand. Here, the effect of ATP and DNA on the thermostability of the MCM from the archaeon Methanothermobacter thermautotrophicus was determined. It is shown that the thermostability of the enzyme is dramatically increase (about 10C) in the presence of ATP and DNA. When ATPS was used, instead of ATP, however, no thermal stabilization could be observed. Thus, the results suggest that ATP hydrolysis is required for MCM stabilization in the presence of DNA. It was also found that MCM stabilization is dependent upon the presence of the oligonucleotide.Citation
ACS Biochemistry
Pub Type
Journals
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Keywords
Archea, ATP, differential scanning calorimetry, DNA, Minichromosome maintenance helicase, thermodynamics
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Created February 25, 2009, Updated August 1, 2025