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Nucleic Acids Research Advance Access originally published online on March 2, 2009
Nucleic Acids Research 2009 37(7):2395-2404; doi:10.1093/nar/gkp092
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Nucleic Acids Research, 2009, Vol. 37, No. 7 2395-2404
© 2009 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Structural Biology

A novel zinc-binding fold in the helicase interaction domain of the Bacillus subtilis DnaI helicase loader

Karin V. Loscha1, Kristaps Jaudzems2, Charikleia Ioannou3, Xun-Cheng Su1, Flynn R. Hill3, Gottfried Otting1, Nicholas E. Dixon1,3 and Edvards Liepinsh2,*

1Research School of Chemistry, Australian National University, Canberra ACT 0200, Australia, 2Institute of Organic Synthesis, Aizkraukles iela 21, Riga, LV 1006, Latvia and 3School of Chemistry, University of Wollongong, NSW 2522, Australia

*To whom correspondence should be addressed. Tel: +371 6701 4817; Fax: +371 6755 0338; Email: edv{at}osi.lv

Received December 18, 2008. Revised January 15, 2009. Accepted February 2, 2009.

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.

The authors wish it to be known that, in their opinion, the first three authors should be regarded as joint First Authors.


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