Stimulation of MCM helicase activity by a Cdc6 protein in the archaeon Thermoplasma acidophilum. Export

@article{citeulike:2755798, abstract = {Replicative DNA helicases are ring-shaped hexamers that play an essential role in chromosomal DNA replication. They unwind the two strands of the duplex DNA and provide the single-stranded (ss) DNA substrate for the polymerase. The minichromosome maintenance (MCM) proteins are thought to function as the replicative helicases in eukarya and archaea. The proteins of only a few archaeal organisms have been studied and revealed that although all have similar amino acid sequences and overall structures they differ in their biochemical properties. In this report the biochemical properties of the MCM protein from the archaeon Thermoplasma acidophilum is described. The enzyme has weak helicase activity on a substrate containing only a 3'-ssDNA overhang region and the protein requires a forked DNA structure for efficient helicase activity. It was also found that the helicase activity is stimulated by one of the two T.acidophilum Cdc6 homologues. This is an interesting observation as it is in sharp contrast to observations made with MCM and Cdc6 homologues from other archaea in which the helicase activity is inhibited when bound to Cdc6.}, address = {Department of Biology, University of Bergen, PO Box 7800, N-5020 Bergen, Norway.}, author = {Haugland, G. T. and Shin, J. H. and Birkeland, N. K. and Kelman, Z.}, citeulike-article-id = {2755798}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/17108356}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=17108356}, issn = {1362-4962}, journal = {Nucleic acids research}, keywords = {cdc6}, number = {21}, pages = {6337--6344}, posted-at = {2008-05-05 10:20:42}, priority = {2}, title = {Stimulation of MCM helicase activity by a Cdc6 protein in the archaeon Thermoplasma acidophilum.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/17108356}, volume = {34}, year = {2006} }

TY - JOUR ID - citeulike:2755798 L3 - citeulike-article-id:2755798 N2 - Replicative DNA helicases are ring-shaped hexamers that play an essential role in chromosomal DNA replication. They unwind the two strands of the duplex DNA and provide the single-stranded (ss) DNA substrate for the polymerase. The minichromosome maintenance (MCM) proteins are thought to function as the replicative helicases in eukarya and archaea. The proteins of only a few archaeal organisms have been studied and revealed that although all have similar amino acid sequences and overall structures they differ in their biochemical properties. In this report the biochemical properties of the MCM protein from the archaeon Thermoplasma acidophilum is described. The enzyme has weak helicase activity on a substrate containing only a 3'-ssDNA overhang region and the protein requires a forked DNA structure for efficient helicase activity. It was also found that the helicase activity is stimulated by one of the two T.acidophilum Cdc6 homologues. This is an interesting observation as it is in sharp contrast to observations made with MCM and Cdc6 homologues from other archaea in which the helicase activity is inhibited when bound to Cdc6. IS - 21 JF - Nucleic acids research SN - 1362-4962 AD - Department of Biology, University of Bergen, PO Box 7800, N-5020 Bergen, Norway. EP - 6344 TI - Stimulation of MCM helicase activity by a Cdc6 protein in the archaeon Thermoplasma acidophilum. VL - 34 SP - 6337 KW - cdc6 AU - Haugland, GT AU - Shin, JH AU - Birkeland, NK AU - Kelman, Z PY - 2006/// UR - http://view.ncbi.nlm.nih.gov/pubmed/17108356 ER -