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Unwinding the structure and function of the archaeal MCM helicase
Author(s) -
Sakakibara Nozomi,
Kelman Lori M.,
Kelman Zvi
Publication year - 2009
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2009.06663.x
Subject(s) - helicase , biology , minichromosome maintenance , archaea , dna replication , sulfolobus , replisome , primase , microbiology and biotechnology , rna helicase a , dna , prokaryotic dna replication , genetics , eukaryotic dna replication , biochemistry , gene , rna , reverse transcriptase
Summary During chromosomal DNA replication, the replicative helicase unwinds the duplex DNA to provide the single‐stranded DNA substrate for the polymerase. In archaea, the replicative helicase is the minichromosome maintenance (MCM) complex. The enzyme utilizes the energy of ATP hydrolysis to translocate along one strand of the duplex and unwind the complementary strand. Much progress has been made in elucidating structure and function since the first report on the biochemical properties of an archaeal MCM protein in 1999. We now know the biochemical and structural properties of the enzyme from several archaeal species and some of the mechanisms by which the enzyme is regulated. This review summarizes recent studies on the archaeal MCM protein and discusses the implications for helicase function and DNA replication in archaea.