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Publikācija: A Novel Zinc-Binding Fold in the Helicase Intreraction Domain of Bacillus Subtilis Dnai Helicase Loader

Publication Type Scientific article indexed in ERIH database, in INT1 or INT2 category journals
Funding for basic activity Unknown
Defending: ,
Publication language English (en)
Title in original language A Novel Zinc-Binding Fold in the Helicase Intreraction Domain of Bacillus Subtilis Dnai Helicase Loader
Field of research 1. Natural sciences
Sub-field of research 1.4 Chemical sciences
Authors Karin Loscha
Kristaps Jaudzems
Charikleia Ioannou
Xun-Cheng Su
Flynn R. Hill
Gottfried Otting
Nicholas Dixon
Edvards Liepiņš
Keywords chemistry ; bioinformatics and computational biology ; genetics and genomics ; molecular and cell biology
Abstract The helicase loader protein DnaI (the Bacillus subtilis homologue of Escherichia coli DnaC) is required to load the hexameric helicase DnaC (the B. subtilis homologue of E. coli DnaB) onto DNA at the start of replication. While the C-terminal domain of DnaI belongs to the structurally well-characterized AAA+ family of ATPases, the structure of the N-terminal domain, DnaI-N, has no homology to a known structure. Three-dimensional structure determination by nuclear magnetic resonance (NMR) spectroscopy shows that DnaI presents a novel fold containing a structurally important zinc ion. Surface plasmon resonance experiments indicate that DnaI-N is largely responsible for binding of DnaI to the hexameric helicase from B. stearothermophilus, which is a close homologue of the corresponding much less stable B. subtilis helicase.
DOI: 10.1093/nar/gkp092
Hyperlink: http://nar.oxfordjournals.org/content/37/7/2395 
Reference Loscha, K., Jaudzems, K., Ioannou, C., Su, X., Hill, F., Otting, G., Dixon, N., Liepiņš, E. A Novel Zinc-Binding Fold in the Helicase Intreraction Domain of Bacillus Subtilis Dnai Helicase Loader. Nucleic Acids Research, 2009, Vol.37, No.7, pp.2395-2404. e-ISSN 1362-4962. ISSN 0305-1048. Available from: doi:10.1093/nar/gkp092
ID 7152