The GINS complex from the thermophilic archaeon, <Emphasis Type="Italic">Thermoplasma acidophilum</Emphasis> may function as a homotetramer in DNA replication |
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Authors: | Hiromi Ogino Sonoko Ishino Kouta Mayanagi Gyri Teien Haugland Nils-Kåre Birkeland Akihiko Yamagishi Yoshizumi Ishino |
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Institution: | (1) Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, 6-10-1 Hakozaki, Higashi-ku, Fukuoka Fukuoka, 812-8581, Japan;(2) Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan;(3) Department of Biology, University of Bergen, Bergen, Norway;(4) Department of Biology and Centre for Geobiology, University of Bergen, Bergen, Norway;(5) Department of Molecular Biology, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo, Japan;(6) BIRD-Japan Science and Technology Agency, Fukuoka 812-8581, Japan; |
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Abstract: | The eukaryotic GINS heterotetramer, consisting of Sld5, Psf1, Psf2, and Psf3, participates in “CMG complex” formation with
mini-chromosome maintenance (MCM) and Cdc45 as a key component of a replicative helicase. There are only two homologs of the
GINS proteins in Archaea, and these proteins, Gins51 and Gins23, form a heterotetrameric GINS with a 2:2 molar ratio. The
Pyrococcus furiosus GINS stimulates the ATPase and helicase activities of its cognate MCM, whereas the Sulfolobus solfataricus GINS does not affect those activities of its cognate MCM, although the proteins bind each other. Intriguingly, Thermoplasma acidophilum, as well as many euryarchaea, have only one gene encoding the sequence homologous to that of archaeal Gins protein (Gins51)
on the genome. In this study, we investigated the biochemical properties of the gene product (TaGins51). A gel filtration
and electron microscopy revealed that TaGins51 forms a homotetramer. A physical interaction between TaGins51 and TaMcm was
detected by a surface plasmon resonance analysis. Unexpectedly, TaGins51 inhibited the ATPase activity, but did not affect
the helicase activity of its cognate MCM. These results suggest that another factor is required to form a stable helicase
complex with MCM and GINS at the replication fork in T. acidophilum cells. |
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