Nucleic Acids Research, 1993, Vol. 21, No. 11 2541-2547
© 1993
SURVEY AND SUMMARY |
A common set of conserved motifs in a vast variety of putative nucleic acid-dependent ATPases including MCM proteins involved in the initiation of eukaryotic DNA replication
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health Bldg. 38A, 8600 Rockville Pike, Bethesda, MD 20894, USA
Received April 1, 1993. Revised May 6, 1993. Accepted May 6, 1993.
A new superfamily of (putative) DNA-dependent ATPases is described that includes the ATPase domains of prokaryotic NtrC-related transcription regulators, MCM proteins involved in the initiation of eukaryotic DNA replication, and a group of uncharacterized bacterial and chloroplast proteins. MCM proteins are shown to contain a modified form of the ATP-binding motif and are predicted to mediate ATP-dependent opening of double-stranded DNA in the replication origins. In a second line of investigation, it is demonstrated that the products of unidentified open reading frames from Marchantia mitochondria and from yeast, and a domain of a baculovirus protein involved in viral DNA replication are related to the superfamily III of DNA and RNA helicases that previously has been known to include only proteins of small viruses. Comparison of the multiple alignments showed that the proteins of the NtrC superfamily and the helicases of superfamily III share three related sequence motifs tightly packed in the ATPase domain that consists of 100–150 amino acid residues. A similar array of conserved motifs is found in the family of DnaA-related ATPases. It is hypothesized that the three large groups of nucleic acid-dependent ATPases have similar structure of the core ATPase domain and have evolved from a common ancestor.
* On leave from Institute of Microbiology, Russian Academy of Sciences, 117811 Moscow, Russia
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J. P. J. Chong, M. K. Hayashi, M. N. Simon, R.-M. Xu, and B. Stillman A double-hexamer archaeal minichromosome maintenance protein is an ATP-dependent DNA helicase PNAS, February 15, 2000; 97(4): 1530 - 1535. [Abstract] [Full Text] [PDF]
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C. J. DaFonseca, F. Shu, and J. J. Zhang Identification of two residues in MCM5 critical for the assembly of MCM complexes and Stat1-mediated transcription activation in response to IFN-gamma PNAS, March 13, 2001; 98(6): 3034 - 3039. [Abstract] [Full Text] [PDF]
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